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3d4c
From Proteopedia
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[[Image:3d4c.png|left|200px]] | [[Image:3d4c.png|left|200px]] | ||
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{{STRUCTURE_3d4c| PDB=3d4c | SCENE= }} | {{STRUCTURE_3d4c| PDB=3d4c | SCENE= }} | ||
===ZP-N domain of mammalian sperm receptor ZP3 (crystal form I)=== | ===ZP-N domain of mammalian sperm receptor ZP3 (crystal form I)=== | ||
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{{ABSTRACT_PUBMED_19052627}} | {{ABSTRACT_PUBMED_19052627}} | ||
==About this Structure== | ==About this Structure== | ||
| - | [[3d4c]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | [[3d4c]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D4C OCA]. |
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:019052627</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:016600035</ref><references group="xtra"/> |
| - | [[Category: | + | [[Category: Mus musculus]] |
[[Category: Jovine, L.]] | [[Category: Jovine, L.]] | ||
[[Category: Monne, M.]] | [[Category: Monne, M.]] | ||
Revision as of 13:21, 6 February 2013
ZP-N domain of mammalian sperm receptor ZP3 (crystal form I)
Template:ABSTRACT PUBMED 19052627
About this Structure
3d4c is a 1 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
- 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
- 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
- Jovine L, Janssen WG, Litscher ES, Wassarman PM. The PLAC1-homology region of the ZP domain is sufficient for protein polymerisation. BMC Biochem. 2006 Apr 6;7:11. PMID:16600035 doi:http://dx.doi.org/10.1186/1471-2091-7-11
Categories: Mus musculus | Jovine, L. | Monne, M. | Biodiversity | Cell adhesion | Egg coat | Egg-sperm interaction | Extracellular matrix | Fertilization | Glycoprotein | Immunoglobulin-like fold | Infertility | Oocyte | Receptor | Secreted | Speciation | Species-specific gamete recognition | Transmembrane | Vitelline envelope | Zona pellucida | Zp domain
