3nk3
From Proteopedia
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===Crystal structure of full-length sperm receptor ZP3 at 2.6 A resolution=== | ===Crystal structure of full-length sperm receptor ZP3 at 2.6 A resolution=== | ||
+ | {{ABSTRACT_PUBMED_20970175}} | ||
- | + | ==Function== | |
- | + | [[http://www.uniprot.org/uniprot/P79762_CHICK P79762_CHICK]] Component of the zona pellucida, which mediates species-specific sperm binding. Directly binds to sperm. Important for egg fertilization.<ref>PMID:15115720</ref> <ref>PMID:20970175</ref> | |
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==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
- | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:020970175</ref><ref group="xtra">PMID:007418009</ref><ref group="xtra">PMID:012021773</ref><ref group="xtra">PMID:015079052</ref><ref group="xtra">PMID:015952882</ref><ref group="xtra">PMID:019052627</ref><references group="xtra"/><references/> |
[[Category: Gallus gallus]] | [[Category: Gallus gallus]] | ||
[[Category: Jovine, L.]] | [[Category: Jovine, L.]] |
Revision as of 12:03, 24 April 2013
Contents |
Crystal structure of full-length sperm receptor ZP3 at 2.6 A resolution
Template:ABSTRACT PUBMED 20970175
Function
[P79762_CHICK] Component of the zona pellucida, which mediates species-specific sperm binding. Directly binds to sperm. Important for egg fertilization.[1] [2]
About this Structure
3nk3 is a 4 chain structure with sequence from Gallus gallus. Full crystallographic information is available from OCA.
Reference
- Han L, Monne M, Okumura H, Schwend T, Cherry AL, Flot D, Matsuda T, Jovine L. Insights into egg coat assembly and egg-sperm interaction from the X-ray structure of full-length ZP3. Cell. 2010 Oct 29;143(3):404-15. Epub 2010 Oct 21. PMID:20970175 doi:10.1016/j.cell.2010.09.041
- Bleil JD, Wassarman PM. Mammalian sperm-egg interaction: identification of a glycoprotein in mouse egg zonae pellucidae possessing receptor activity for sperm. Cell. 1980 Jul;20(3):873-82. PMID:7418009
- Jovine L, Qi H, Williams Z, Litscher E, Wassarman PM. The ZP domain is a conserved module for polymerization of extracellular proteins. Nat Cell Biol. 2002 Jun;4(6):457-61. PMID:12021773 doi:10.1038/ncb802
- Jovine L, Qi H, Williams Z, Litscher ES, Wassarman PM. A duplicated motif controls assembly of zona pellucida domain proteins. Proc Natl Acad Sci U S A. 2004 Apr 20;101(16):5922-7. Epub 2004 Apr 12. PMID:15079052 doi:http://dx.doi.org/10.1073/pnas.0401600101
- Jovine L, Darie CC, Litscher ES, Wassarman PM. Zona pellucida domain proteins. Annu Rev Biochem. 2005;74:83-114. PMID:15952882 doi:http://dx.doi.org/10.1146/annurev.biochem.74.082803.133039
- Monne M, Han L, Schwend T, Burendahl S, Jovine L. Crystal structure of the ZP-N domain of ZP3 reveals the core fold of animal egg coats. Nature. 2008 Dec 4;456(7222):653-7. PMID:19052627 doi:10.1038/nature07599
- ↑ Bausek N, Ruckenbauer HH, Pfeifer S, Schneider WJ, Wohlrab F. Interaction of sperm with purified native chicken ZP1 and ZPC proteins. Biol Reprod. 2004 Aug;71(2):684-90. Epub 2004 Apr 28. PMID:15115720 doi:10.1095/biolreprod.104.028605
- ↑ Han L, Monne M, Okumura H, Schwend T, Cherry AL, Flot D, Matsuda T, Jovine L. Insights into egg coat assembly and egg-sperm interaction from the X-ray structure of full-length ZP3. Cell. 2010 Oct 29;143(3):404-15. Epub 2010 Oct 21. PMID:20970175 doi:10.1016/j.cell.2010.09.041
Categories: Gallus gallus | Jovine, L. | Monne , M. | Biodiversity | Cell adhesion | Core-1 | Egg coat | Egg-sperm interaction | Ehp | External hydrophobic patch | Extracellular matrix | Fertilization | Glycoprotein | Ihp | Immunoglobulin-like fold | Infertility | Internal hydrophobic patch | O-linked carbohydrate | Oocyte | Receptor | Secreted | Speciation | Species-specific gamete recognition | Sperm-combining site | T-antigen | Transmembrane | Vitelline envelope | Zona pellucida | Zp domain | Zp module