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63-640: 836 12367 ENSG00000164305 ENSMUSG00000031628 P42574 P70677 NM_004346 NM_032991 NM_009810 NM_001284409 NP_001341710 NP_001341711 NP_001341712 NP_001341713 NP_001271338 NP_033940 Caspase-3 is a caspase protein that interacts with caspase-8 and caspase-9 . It is encoded by the CASP3 gene. CASP3 orthologs have been identified in numerous mammals for which complete genome data are available. Unique orthologs are also present in birds , lizards , lissamphibians , and teleosts . The CASP3 protein

126-406: A cysteine residue (Cys-163) and histidine residue (His-121) that stabilize the peptide bond cleavage of a protein sequence to the carboxy-terminal side of an aspartic acid when it is part of a particular 4-amino acid sequence. This specificity allows caspases to be incredibly selective, with a 20,000-fold preference for aspartic acid over glutamic acid . A key feature of caspases in the cell

189-399: A cause of Alzheimer's . Its structure has yet to be determined in full, but recent data suggest that it may resemble an unusual two-strand β-helix. The side chains from the amino acid residues found in a β-sheet structure may also be arranged such that many of the adjacent sidechains on one side of the sheet are hydrophobic, while many of those adjacent to each other on the alternate side of

252-418: A cause of tumor development. Tumor growth can occur by a combination of factors, including a mutation in a cell cycle gene which removes the restraints on cell growth, combined with mutations in apoptotic proteins such as caspases that would respond by inducing cell death in abnormally growing cells. Conversely, over-activation of some caspases such as caspase -3 can lead to excessive programmed cell death. This

315-466: A chain reaction, activating several other executioner caspases. Executioner caspases degrade over 600 cellular components in order to induce the morphological changes for apoptosis. Examples of caspase cascade during apoptosis: Pyroptosis is a form of programmed cell death that inherently induces an immune response. It is morphologically distinct from other types of cell death – cells swell up, rupture and release pro-inflammatory cellular contents. This

378-548: A cysteine in its active site nucleophilically attacks and cleaves a target protein only after an aspartic acid residue. As of 2009, there are 12 confirmed caspases in humans and 10 in mice, carrying out a variety of cellular functions. The role of these enzymes in programmed cell death was first identified in 1993, with their functions in apoptosis well characterised. This is a form of programmed cell death, occurring widely during development, and throughout life to maintain cell homeostasis . Activation of caspases ensures that

441-543: A directionality conferred by their N-terminus and C-terminus , β-strands too can be said to be directional. They are usually represented in protein topology diagrams by an arrow pointing toward the C-terminus. Adjacent β-strands can form hydrogen bonds in antiparallel, parallel, or mixed arrangements. In an antiparallel arrangement, the successive β-strands alternate directions so that the N-terminus of one strand

504-528: A drug target. For example, inflammatory caspase-1 has been implicated in causing autoimmune diseases ; drugs blocking the activation of Caspase-1 have been used to improve the health of patients. Additionally, scientists have used caspases as cancer therapy to kill unwanted cells in tumors. Most caspases play a role in programmed cell death. These are summarized in the table below. The enzymes are sub classified into three types: Initiator, Executioner and Inflammatory. Note that in addition to apoptosis, caspase-8

567-405: A heterodimer, which in turn interacts with another heterodimer to form the full 12-stranded beta-sheet structure surrounded by alpha-helices that is unique to caspases. When the heterodimers align head-to-tail with each other, an active site is positioned at each end of the molecule formed by residues from both participating subunits, though the necessary Cys-163 and His-121 residues are found on

630-483: A large and small subunit. This cleavage allows the active-site loops to take up a conformation favourable for enzymatic activity. Cleavage of Initiator and Executioner caspases occur by different methods outlined in the table below. Caspase-8 Caspase Caspase-3 Apoptosis is a form of programmed cell death where the cell undergoes morphological changes, to minimize its effect on surrounding cells to avoid inducing an immune response. The cell shrinks and condenses -

693-780: A mixed bonding pattern, with a parallel strand on one side and an antiparallel strand on the other. Such arrangements are less common than a random distribution of orientations would suggest, suggesting that this pattern is less stable than the anti-parallel arrangement, however bioinformatic analysis always struggles with extracting structural thermodynamics since there are always numerous other structural features present in whole proteins. Also proteins are inherently constrained by folding kinetics as well as folding thermodynamics, so one must always be careful in concluding stability from bioinformatic analysis. The hydrogen bonding of β-strands need not be perfect, but can exhibit localized disruptions known as β-bulges . The hydrogen bonds lie roughly in

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756-736: A motif, suggesting that a smaller number of strands may be unstable, however it is also fundamentally more difficult for parallel β-sheets to form because strands with N and C termini aligned necessarily must be very distant in sequence . There is also evidence that parallel β-sheet may be more stable since small amyloidogenic sequences appear to generally aggregate into β-sheet fibrils composed of primarily parallel β-sheet strands, where one would expect anti-parallel fibrils if anti-parallel were more stable. In parallel β-sheet structure, if two atoms C i and C j are adjacent in two hydrogen-bonded β-strands, then they do not hydrogen bond to each other; rather, one residue forms hydrogen bonds to

819-519: A multiprotein complex called the NLRP3 inflammasome . The pro-caspase-1 is brought into close proximity with other pro-caspase molecule in order to dimerise and undergo auto-proteolytic cleavage. Some pathogenic signals that lead to Pyroptosis by Caspase-1 are listed below: Pyroptosis by Caspase-4 and Caspase-5 in humans and Caspase-11 in mice These caspases have the ability to induce direct pyroptosis when lipopolysaccharide (LPS) molecules (found in

882-457: A range of pathogenic ligands. Some mediators of Caspase-1 activation are: NOD-like Leucine Rich Repeats (NLRs), AIM2 -Like Receptors (ALRs), Pyrin and IFI16 . These proteins allow caspase-1 activation by forming a multiprotein activating complex called Inflammasomes. For example, a NOD Like Leucine Rich Repeat NLRP3 will sense an efflux of potassium ions from the cell. This cellular ion imbalance leads to oligomerisation of NLRP3 molecules to form

945-473: A sign of a recent myocardial infarction . It is now being shown that caspase-3 may play a role in embryonic and hematopoietic stem cell differentiation. Caspase Caspases ( c ysteine- asp artic prote ases , c ysteine asp art ases or c ysteine-dependent asp artate-directed prote ases ) are a family of protease enzymes playing essential roles in programmed cell death . They are named caspases due to their specific cysteine protease activity –

1008-400: A specific site, preventing XIAP from being able to bind to inhibit caspase-9 activity. Caspase 3 has been shown to interact with: Caspase-3 has been found to be necessary for normal brain development as well as its typical role in apoptosis, where it is responsible for chromatin condensation and DNA fragmentation. Elevated levels of a fragment of Caspase-3, p17, in the bloodstream is

1071-430: A tight turn or a β-bulge loop . Individual strands can also be linked in more elaborate ways with longer loops that may contain α-helices . The Greek key motif consists of four adjacent antiparallel strands and their linking loops. It consists of three antiparallel strands connected by hairpins, while the fourth is adjacent to the first and linked to the third by a longer loop. This type of structure forms easily during

1134-408: A β-sheet describes the order of hydrogen-bonded β-strands along the backbone. For example, the flavodoxin fold has a five-stranded, parallel β-sheet with topology 21345; thus, the edge strands are β-strand 2 and β-strand 5 along the backbone. Spelled out explicitly, β-strand 2 is H-bonded to β-strand 1, which is H-bonded to β-strand 3, which is H-bonded to β-strand 4, which is H-bonded to β-strand 5,

1197-430: Is a common motif of the regular protein secondary structure . Beta sheets consist of beta strands ( β-strands ) connected laterally by at least two or three backbone hydrogen bonds , forming a generally twisted, pleated sheet. A β-strand is a stretch of polypeptide chain typically 3 to 10 amino acids long with backbone in an extended conformation . The supramolecular association of β-sheets has been implicated in

1260-428: Is a member of the c ysteine- asp artic acid prote ase ( caspase ) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis . Caspases exist as inactive proenzymes that undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme . This protein cleaves and activates caspases 6 and 7 ; and

1323-545: Is absolutely required while variations at other three positions can be tolerated. Caspase substrate specificity has been widely used in caspase based inhibitor and drug design. Caspase-3, in particular, (also known as CPP32/Yama/apopain) is formed from a 32 kDa zymogen that is cleaved into 17 kDa and 12 kDa subunits. When the procaspase is cleaved at a particular residue, the active heterotetramer can then be formed by hydrophobic interactions, causing four anti-parallel beta-sheets from p17 and two from p12 to come together to make

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1386-558: Is adjacent to the C-terminus of the next. This is the arrangement that produces the strongest inter-strand stability because it allows the inter-strand hydrogen bonds between carbonyls and amines to be planar, which is their preferred orientation. The peptide backbone dihedral angles ( φ ,  ψ ) are about (–140°, 135°) in antiparallel sheets. In this case, if two atoms C i and C j are adjacent in two hydrogen-bonded β-strands, then they form two mutual backbone hydrogen bonds to each other's flanking peptide groups ; this

1449-458: Is also required for the inhibition of another form of programmed cell death called necroptosis. Caspase-14 plays a role in epithelial cell keratinocyte differentiation and can form an epidermal barrier that protects against dehydration and UVB radiation. Caspases are synthesised as inactive zymogens (pro-caspases) that are only activated following an appropriate stimulus. This post-translational level of control allows rapid and tight regulation of

1512-518: Is common in β-sheets and can be found in several structural architectures including β-barrels and β-propellers . The vast majority of β-meander regions in proteins are found packed against other motifs or sections of the polypeptide chain, forming portions of the hydrophobic core that canonically drives formation of the folded structure.   However, several notable exceptions include the Outer Surface Protein A (OspA) variants and

1575-542: Is connected to both by hydrogen bonds. There are four possible strand topologies for single Ψ-loops. This motif is rare as the process resulting in its formation seems unlikely to occur during protein folding. The Ψ-loop was first identified in the aspartic protease family. β-sheets are present in all-β , α+β and α/β domains, and in many peptides or small proteins with poorly defined overall architecture. All-β domains may form β-barrels , β-sandwiches , β-prisms, β-propellers , and β-helices . The topology of

1638-443: Is done in response to a range of stimuli including microbial infections as well as heart attacks (myocardial infarctions). Caspase-1, Caspase-4 and Caspase-5 in humans, and Caspase-1 and Caspase-11 in mice play important roles in inducing cell death by pyroptosis. This limits the life and proliferation time of intracellular and extracellular pathogens. Caspase-1 activation is mediated by a repertoire of proteins, allowing detection of

1701-488: Is induced by caspases and in fungi and plants, apoptosis is induced by arginine and lysine-specific caspase like proteases called metacaspases. Homology searches revealed a close homology between caspases and the caspase-like proteins of Reticulomyxa (a unicellular organism). The phylogenetic study indicates that divergence of caspase and metacaspase sequences occurred before the divergence of eukaryotes. Beta-sheet The beta sheet ( β-sheet , also β-pleated sheet )

1764-409: Is initiated by dimerisation, which is facilitated by binding to adaptor proteins via protein–protein interaction motifs that are collectively referred to as death folds . The death folds are located in a structural domain of the caspases known as the pro-domain, which is larger in those caspases that contain death folds than in those that do not. The pro-domain of the intrinsic initiator caspases and

1827-487: Is known as a close pair of hydrogen bonds. In a parallel arrangement, all of the N-termini of successive strands are oriented in the same direction; this orientation may be slightly less stable because it introduces nonplanarity in the inter-strand hydrogen bonding pattern. The dihedral angles ( φ ,  ψ ) are about (–120°, 115°) in parallel sheets. It is rare to find less than five interacting parallel strands in

1890-486: Is roughly 5 Å (0.50 nm). However, β-strands are rarely perfectly extended; rather, they exhibit a twist. The energetically preferred dihedral angles near ( φ ,  ψ ) = (–135°, 135°) (broadly, the upper left region of the Ramachandran plot ) diverge significantly from the fully extended conformation ( φ ,  ψ ) = (–180°, 180°). The twist is often associated with alternating fluctuations in

1953-449: Is seen in several neurodegenerative diseases where neural cells are lost, such as Alzheimer's disease . Caspases involved with processing inflammatory signals are also implicated in disease. Insufficient activation of these caspases can increase an organism's susceptibility to infection, as an appropriate immune response may not be activated. The integral role caspases play in cell death and disease has led to research on using caspases as

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2016-562: Is that they are present as zymogens , termed procaspases, which are inactive until a biochemical change causes their activation. Each procaspase has an N-terminal large subunit of about 20 kDa followed by a smaller subunit of about 10 kDa, called p20 and p10, respectively. Under normal circumstances, caspases recognize tetra-peptide sequences on their substrates and hydrolyze peptide bonds after aspartic acid residues. Caspase 3 and caspase 7 share similar substrate specificity by recognizing tetra-peptide motif Asp-x-x-Asp. The C-terminal Asp

2079-652: Is the introduction of granzyme B , which can activate initiator caspases, into cells targeted for apoptosis by killer T cells . This extrinsic activation then triggers the hallmark caspase cascade characteristic of the apoptotic pathway, in which caspase-3 plays a dominant role. In intrinsic activation, cytochrome c from the mitochondria works in combination with caspase-9 , apoptosis-activating factor 1 ( Apaf-1 ), and ATP to process procaspase-3. These molecules are sufficient to activate caspase-3 in vitro, but other regulatory proteins are necessary in vivo . Mangosteen ( Garcinia mangostana ) extract has been shown to inhibit

2142-560: The N−H groups in the backbone of one strand establish hydrogen bonds with the C=O groups in the backbone of the adjacent strands. In the fully extended β-strand, successive side chains point straight up and straight down in an alternating pattern. Adjacent β-strands in a β-sheet are aligned so that their C atoms are adjacent and their side chains point in the same direction. The "pleated" appearance of β-strands arises from tetrahedral chemical bonding at

2205-487: The Raman spectroscopy and analyzed with the quasi-continuum model. A β-helix is formed from repeating structural units consisting of two or three short β-strands linked by short loops. These units "stack" atop one another in a helical fashion so that successive repetitions of the same strand hydrogen-bond with each other in a parallel orientation. See the β-helix article for further information. In lefthanded β-helices,

2268-774: The TIM barrel ). β-Barrels are often described by their stagger or shear . Some open β-sheets are very curved and fold over on themselves (as in the SH3 domain ) or form horseshoe shapes (as in the ribonuclease inhibitor ). Open β-sheets can assemble face-to-face (such as the β-propeller domain or immunoglobulin fold ) or edge-to-edge, forming one big β-sheet. β-pleated sheet structures are made from extended β-strand polypeptide chains, with strands linked to their neighbours by hydrogen bonds . Due to this extended backbone conformation, β-sheets resist stretching . β-sheets in proteins may carry out low-frequency accordion-like motion as observed by

2331-533: The cytoskeleton will collapse, and the nuclear envelope disassembles the DNA fragments up. This results in the cell forming self-enclosed bodies called ' blebs ', to avoid release of cellular components into the extracellular medium. Additionally, the cell membrane phospholipid content is altered, which makes the dying cell more susceptible to phagocytic attack and removal. Apoptotic caspases are subcategorised as: Once initiator caspases are activated, they produce

2394-453: The dihedral angles to prevent the individual β-strands in a larger sheet from splaying apart. A good example of a strongly twisted β-hairpin can be seen in the protein BPTI . The side chains point outwards from the folds of the pleats, roughly perpendicularly to the plane of the sheet; successive amino acid residues point outwards on alternating faces of the sheet. Because peptide chains have

2457-442: The edge strands in β-sheets, presumably to avoid the "edge-to-edge" association between proteins that might lead to aggregation and amyloid formation. A very simple structural motif involving β-sheets is the β-hairpin , in which two antiparallel strands are linked by a short loop of two to five residues, of which one is frequently a glycine or a proline , both of which can assume the dihedral-angle conformations required for

2520-473: The pectate lyase enzyme shown at left or P22 phage tailspike protein , have a less regular cross-section, longer and indented on one of the sides; of the three linker loops, one is consistently just two residues long and the others are variable, often elaborated to form a binding or active site. A two-sided β-helix (right-handed) is found in some bacterial metalloproteases ; its two loops are each six residues long and bind stabilizing calcium ions to maintain

2583-400: The protein folding process. It was named after a pattern common to Greek ornamental artwork (see meander ). Due to the chirality of their component amino acids, all strands exhibit right-handed twist evident in most higher-order β-sheet structures. In particular, the linking loop between two parallel strands almost always has a right-handed crossover chirality, which is strongly favored by

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2646-512: The C atom; for example, if a side chain points straight up, then the bonds to the C′ must point slightly downwards, since its bond angle is approximately 109.5°. The pleating causes the distance between C i and C i + 2 to be approximately 6  Å (0.60  nm ), rather than the 7.6 Å (0.76 nm) expected from two fully extended trans peptides . The "sideways" distance between adjacent C atoms in hydrogen-bonded β-strands

2709-518: The Single Layer β-sheet Proteins (SLBPs) which contain single-layer β-sheets in the absence of a traditional hydrophobic core.  These β-rich proteins feature an extended single-layer β-meander β-sheets that are primarily stabilized via inter-β-strand interactions and hydrophobic interactions present in the turn regions connecting individual strands. The psi-loop (Ψ-loop) motif consists of two antiparallel strands with one strand in between that

2772-546: The activation of caspase 3 in B-amyloid treated human neuronal cells. One means of caspase inhibition is through the IAP (inhibitor of apoptosis) protein family, which includes c-IAP1, c-IAP2, XIAP , and ML-IAP. XIAP binds and inhibits initiator caspase-9, which is directly involved in the activation of executioner caspase-3. During the caspase cascade, however, caspase-3 functions to inhibit XIAP activity by cleaving caspase-9 at

2835-483: The amino acids in order to build accurate models, especially since he did not then know that the peptide bond was planar. A refined version was proposed by Linus Pauling and Robert Corey in 1951. Their model incorporated the planarity of the peptide bond which they previously explained as resulting from keto-enol tautomerization . The majority of β-strands are arranged adjacent to other strands and form an extensive hydrogen bond network with their neighbors in which

2898-408: The apoptotic cell both by extrinsic (death ligand) and intrinsic (mitochondrial) pathways. The zymogen feature of caspase-3 is necessary because if unregulated, caspase activity would kill cells indiscriminately. As an executioner caspase, the caspase-3 zymogen has virtually no activity until it is cleaved by an initiator caspase after apoptotic signaling events have occurred. One such signaling event

2961-625: The cell wall of gram negative bacteria) are found in the cytoplasm of the host cell. For example, Caspase 4 acts as a receptor and is proteolytically activated, without the need of an inflammasome complex or Caspase-1 activation. A crucial downstream substrate for pyroptotic caspases is Gasdermin D (GSDMD) Inflammation is a protective attempt by an organism to restore a homeostatic state, following disruption from harmful stimulus, such as tissue damage or bacterial infection. Caspase-1, Caspase-4, Caspase-5 and Caspase-11 are considered 'Inflammatory Caspases'. H. Robert Horvitz initially established

3024-800: The cellular components are degraded in a controlled manner, carrying out cell death with minimal effect on surrounding tissues . Caspases have other identified roles in programmed cell death such as pyroptosis , necroptosis and PANoptosis . These forms of cell death are important for protecting an organism from stress signals and pathogenic attack. Caspases also have a role in inflammation, whereby it directly processes pro-inflammatory cytokines such as pro- IL1β . These are signalling molecules that allow recruitment of immune cells to an infected cell or tissue. There are other identified roles of caspases such as cell proliferation, tumor suppression, cell differentiation, neural development and axon guidance and ageing. Caspase deficiency has been identified as

3087-463: The enzyme. Activation involves dimerization and often oligomerisation of pro-caspases, followed by cleavage into a small subunit and large subunit. The large and small subunit associate with each other to form an active heterodimer caspase. The active enzyme often exists as a heterotetramer in the biological environment, where a pro-caspase dimer is cleaved together to form a heterotetramer. The activation of initiator caspases and inflammatory caspases

3150-402: The formation of the fibrils and protein aggregates observed in amyloidosis , Alzheimer's disease and other proteinopathies . The first β-sheet structure was proposed by William Astbury in the 1930s. He proposed the idea of hydrogen bonding between the peptide bonds of parallel or antiparallel extended β-strands. However, Astbury did not have the necessary data on the bond geometry of

3213-409: The importance of caspases in apoptosis and found that the ced-3 gene is required for the cell death that took place during the development of the nematode C. elegans . Horvitz and his colleague Junying Yuan found in 1993 that the protein encoded by the ced-3 gene is cysteine protease with similar properties to the mammalian interleukin-1-beta converting enzyme (ICE) (now known as caspase 1). At

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3276-489: The inflammatory caspases contains a single death fold known as caspase recruitment domain (CARD), while the pro-domain of the extrinsic initiator caspases contains two death folds known as death effector domains (DED). Multiprotein complexes often form during caspase activation. Some activating multiprotein complexes includes: Once appropriately dimerised, the Caspases cleave at inter domain linker regions, forming

3339-437: The inherent twist of the sheet. This linking loop frequently contains a helical region, in which case it is called a β-α-β motif. A closely related motif called a β-α-β-α motif forms the basic component of the most commonly observed protein tertiary structure , the TIM barrel . A simple supersecondary protein topology composed of two or more consecutive antiparallel β-strands linked together by hairpin loops. This motif

3402-506: The integrity of the structure, using the backbone and the Asp side chain oxygens of a GGXGXD sequence motif. This fold is called a β-roll in the SCOP classification. Some proteins that are disordered or helical as monomers, such as amyloid β (see amyloid plaque ) can form β-sheet-rich oligomeric structures associated with pathological states. The amyloid β protein's oligomeric form is implicated as

3465-499: The other edge strand. In the same system, the Greek key motif described above has a 4123 topology. The secondary structure of a β-sheet can be described roughly by giving the number of strands, their topology, and whether their hydrogen bonds are parallel or antiparallel. β-sheets can be open , meaning that they have two edge strands (as in the flavodoxin fold or the immunoglobulin fold ) or they can be closed β-barrels (such as

3528-455: The p17 (larger) subunit. The catalytic site of caspase-3 involves the thiol group of Cys-163 and the imidazole ring of His-121. His-121 stabilizes the carbonyl group of the key aspartate residue, while Cys-163 attacks to ultimately cleave the peptide bond. Cys-163 and Gly-238 also function to stabilize the tetrahedral transition state of the substrate-enzyme complex through hydrogen bonding . In vitro , caspase-3 has been found to prefer

3591-410: The peptide sequence DEVDG (Asp-Glu-Val-Asp-Gly) with cleavage occurring on the carboxy side of the second aspartic acid residue (between D and G). Caspase-3 is active over a broad pH range that is slightly higher (more basic) than many of the other executioner caspases. This broad range indicates that caspase-3 will be fully active under normal and apoptotic cell conditions. Caspase-3 is activated in

3654-485: The plane of the sheet, with the peptide carbonyl groups pointing in alternating directions with successive residues; for comparison, successive carbonyls point in the same direction in the alpha helix . Large aromatic residues ( tyrosine , phenylalanine , tryptophan ) and β-branched amino acids ( threonine , valine , isoleucine ) are favored to be found in β-strands in the middle of β-sheets. Different types of residues (such as proline ) are likely to be found in

3717-523: The protein itself is processed and activated by caspases 8, 9, and 10 . It is the predominant caspase involved in the cleavage of amyloid-beta 4A precursor protein , which is associated with neuronal death in Alzheimer's disease . Alternative splicing of this gene results in two transcript variants that encode the same protein. Caspase-3 shares many of the typical characteristics common to all currently-known caspases. For example, its active site contains

3780-457: The residues that flank the other (but not vice versa). For example, residue i may form hydrogen bonds to residues j  − 1 and j  + 1; this is known as a wide pair of hydrogen bonds. By contrast, residue j may hydrogen-bond to different residues altogether, or to none at all. The hydrogen bond arrangement in parallel beta sheet resembles that in an amide ring motif with 11 atoms. Finally, an individual strand may exhibit

3843-416: The strands themselves are quite straight and untwisted; the resulting helical surfaces are nearly flat, forming a regular triangular prism shape, as shown for the 1QRE archaeal carbonic anhydrase at right. Other examples are the lipid A synthesis enzyme LpxA and insect antifreeze proteins with a regular array of Thr sidechains on one face that mimic the structure of ice. Righthanded β-helices, typified by

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3906-427: The time, ICE was the only known caspase. Other mammalian caspases were subsequently identified, in addition to caspases in organisms such as fruit fly Drosophila melanogaster . Researchers decided upon the nomenclature of the caspase in 1996. In many instances, a particular caspase had been identified simultaneously by more than one laboratory; each would then give the protein a different name. For example, caspase 3

3969-413: Was variously known as CPP32, apopain and Yama. Caspases, therefore, were numbered in the order in which they were identified. ICE was, therefore, renamed as caspase 1. ICE was the first mammalian caspase to be characterised because of its similarity to the nematode death gene ced-3, but it appears that the principal role of this enzyme is to mediate inflammation rather than cell death. In animals apoptosis

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