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24-450: 22788 ENSG00000188372 ENSMUSG00000004948 P21754 P10761 NM_007155 NM_001110354 NM_011776 NP_001103824 NP_009086 NP_035906 Zona pellucida sperm-binding protein 3 , also known as zona pellucida glycoprotein 3 (Zp-3) or the sperm receptor , is a ZP module -containing protein that in humans is encoded by the ZP3 gene . ZP3 is the glycoprotein in

48-492: A EHP/IHP motif that controls polymerization. The first 3D structure of a homopolymeric ZP module protein filament, native human uromodulin ( UMOD ), was determined by cryo-EM . Additional copies of isolated ZP-N domains are found in the N-terminal region of egg coat protein subunits involved in fertilization in both vertebrates and invertebrates, with the human zona pellucida components ZP1 , ZP2 and ZP4 being

72-497: Is a chemical database of over 400,000 chemicals complete with names, synonyms, and structures . It includes links to NLM and other databases and resources, including links to federal, state and international agencies. The Toxicology and Environmental Health Program was established at the National Library of Medicine in 1967 and is charged with developing computer databases compiled from the medical literature and from

96-796: Is a stub . You can help Misplaced Pages by expanding it . United States National Library of Medicine The United States National Library of Medicine ( NLM ), operated by the United States federal government , is the world's largest medical library . Located in Bethesda, Maryland , the NLM is an institute within the National Institutes of Health . Its collections include more than seven million books , journals , technical reports , manuscripts , microfilms , photographs , and images on medicine and related sciences, including some of

120-406: Is a large protein region of about 260 amino acids. It has been recognised in a variety of receptor-like eukaryotic glycoproteins . All of these molecules are mosaic proteins with a large extracellular region composed of various domains, often followed by either a transmembrane domain and a short cytoplasmic region or by a GPI -anchor. Functional and crystallographic studies revealed that

144-516: Is a major structural component of the ZP and functions in primary binding and stimulation of the sperm acrosome reaction. The nascent protein contains a N-terminal signal peptide sequence, a conserved "ZP domain" module , a consensus furin cleavage site (CFCS), a polymerization-blocking external hydrophobic patch (EHP), and a C-terminal transmembrane domain. Cleavage at the CFCS separates the mature protein from

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192-407: The sea lamprey has seven. X-ray crystallographic studies of the N-terminal half of mammalian ZP3 ( PDB : 3D4C , 3D4G , 3EF7 , 5OSQ ​) as well as its full-length avian homolog ( PDB : 3NK3 , 3NK4 ​) revealed that the protein's ZP module consists of two immunoglobulin-like domains, ZP-N and ZP-C. The latter, which contains EHP as well as a ZP3-specific subdomain, interacts with

216-410: The zona pellucida most important for inducting the acrosome reaction of sperm cells at the beginning of fertilization . The zona pellucida (ZP) is a specialized extracellular matrix that surrounds the oocyte and early embryo. It is composed of three or four glycoproteins (ZP1-4) with various functions during oogenesis, fertilization and preimplantation development. The protein encoded by this gene

240-538: The "ZP domain" region common to all these proteins is a protein polymerization module that consists of two distinct but structurally related immunoglobulin-like domains, ZP-N and ZP-C , separated by an interdomain linker (ITD). The ZP module is located in the C-terminal portion of the extracellular region and – with the exception of non-polymeric family member ENG – contains 8 or 10 conserved Cys residues involved in disulfide bonds. The ZP-C domain contains

264-459: The EHP, allowing it to incorporate into nascent ZP filaments. A variation in the last exon of this gene has previously served as the basis for an additional ZP3 locus; however, sequence and literature review reveals that there is only one full-length ZP3 locus in the human genome. Another locus encoding a bipartite transcript designated POMZP3 contains a duplication of the last four exons of ZP3, including

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288-679: The Internet through the Entrez search engine and Lister Hill National Center For Biomedical Communications . As the United States National Release Center for SNOMED CT , NLM provides SNOMED CT data and resources to licensees of the NLM UMLS Metathesaurus. NLM maintains ClinicalTrials.gov registry for human interventional and observational studies. Additionally NLM runs ChemIDplus, which

312-653: The Journal of Cellular and Molecular Medicine conducted experiments to determine the mechanisms surrounding possible mutations to the ZP gene and how they would impact fertility. By performing whole-exome sequencing they isolated a genome that had a mutation in the ZP3 and the ZP1 genes. They then transfected these genes into HeLa cell cultures and ran a variety of tests to isolate the consequences of these mutations. The authors wrote this regarding their results: “The results indicate that

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360-610: The National Library of Medicine, through the instrumentality of Frank Bradway Rogers , who was the director from 1956 to 1963. The library moved to its current quarters in Bethesda, Maryland , on the campus of the National Institutes of Health, in 1962. Directors from 1945 to present Since 1879, the National Library of Medicine has published the Index Medicus , a monthly guide to articles, in nearly five thousand selected journals. The last issue of Index Medicus

384-644: The ZP proteins 1-4 are properly functioning. Without this interface of proper protein function, sperm binding is inhibited, and fertility is compromised. This article incorporates text from the United States National Library of Medicine , which is in the public domain . This article on a gene on human chromosome 7 is a stub . You can help Misplaced Pages by expanding it . Zona pellucida-like domain The zona pellucida -like domain ( ZP domain / ZP-like domain / ZP module )

408-537: The ZP-N domain of a second molecule to generate an antiparallel homodimeric arrangement required for protein secretion. The Zona Pellucida (ZP) is a complex matrix of glycoprotein that surrounds the oocyte and plays a crucial role in the attachment of sperm during reproduction. Ultimately, through the facilitation of sperm binding and the initiation of the acrosome reaction, the ZP proteins are essential to reproduction and have an important impact on fertility. Research through

432-479: The above described variation, and maps closely to this gene. In mice, ZP3 (more specifically the portion in its exon 7) is the single ZP protein that is sufficient and necessary for sperm binding in vitro , but is insufficient for fertilization in vivo . In humans, ZP1, ZP3, and ZP4 all appear partially responsible for starting the acrosome reaction. Orthologs of these genes are found throughout Vertebrata. The western clawed frog appears to have two orthologs, and

456-404: The best understood. The mollusc " vitelline envelope receptor for egg lysin " (VERL, Q8WR62 ) is found in the vitelline envelope of mollusc eggs and consists of 22 VERL repeats followed by a ZP module. Structural work from 2017 demonstrated that VERL repeats are also ZP-N domains. Humans genes encoding proteins containing this domain include: This membrane protein –related article

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504-714: The history of medicine and the life sciences also are supported by the History of Medicine Division. In April 2008 the current exhibition Against the Odds: Making a Difference in Global Health was launched. National Center for Biotechnology Information is an intramural division within National Library of Medicine that creates public databases in molecular biology, conducts research in computational biology , develops software tools for analyzing molecular and genomic data, and disseminates biomedical information, all for

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528-407: The mutations are involved in the reduced secretion of ZP1 and ZP3 and leading to connection failure of the ZP filaments in vitro. The data suggest a potential that the mutations may be involved in the lacking ZP phenotype, which need to be further investigated in vivo.” (Cao, Qiqi, et al.) It is clear that that the ZP proteins are crucial to expressing a correct ZP phenotype in humans, in which all of

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576-559: Was printed in December 2004, but this information is offered in the freely accessible PubMed , among the more than fifteen million MEDLINE journal article references and abstracts going back to the 1960s and 1.5 million references going back to the 1950s. The National Library of Medicine runs the National Center for Biotechnology Information , which houses biological databases (PubMed among them) that are freely accessible on

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