5ii6: Difference between revisions
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The | ==Crystal structure of the ZP-N1 domain of mouse sperm receptor ZP2 at 0.95 A resolution== | ||
<StructureSection load='5ii6' size='340' side='right' caption='[[5ii6]], [[Resolution|resolution]] 0.95Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5ii6]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5II6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5II6 FirstGlance]. <br> | |||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3d4c|3d4c]], [[3d4g|3d4g]], [[3ef7|3ef7]], [[3nk3|3nk3]], [[3nk4|3nk4]], [[5bup|5bup]]</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ii6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ii6 OCA], [http://pdbe.org/5ii6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ii6 RCSB], [http://www.ebi.ac.uk/pdbsum/5ii6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ii6 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/ZP2_MOUSE ZP2_MOUSE]] The mammalian zona pellucida, which mediates species-specific sperm binding, induction of the acrosome reaction and prevents post-fertilization polyspermy, is composed of three to four glycoproteins, ZP1, ZP2, ZP3, and ZP4. ZP2 may act as a secondary sperm receptor.<ref>PMID:22472438</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Recognition between sperm and the egg surface marks the beginning of life in all sexually reproducing organisms. This fundamental biological event depends on the species-specific interaction between rapidly evolving counterpart molecules on the gametes. We report biochemical, crystallographic, and mutational studies of domain repeats 1-3 of invertebrate egg coat protein VERL and their interaction with cognate sperm protein lysin. VERL repeats fold like the functionally essential N-terminal repeat of mammalian sperm receptor ZP2, whose structure is also described here. Whereas sequence-divergent repeat 1 does not bind lysin, repeat 3 binds it non-species specifically via a high-affinity, largely hydrophobic interface. Due to its intermediate binding affinity, repeat 2 selectively interacts with lysin from the same species. Exposure of a highly positively charged surface of VERL-bound lysin suggests that complex formation both disrupts the organization of egg coat filaments and triggers their electrostatic repulsion, thereby opening a hole for sperm penetration and fusion. | |||
Structural Basis of Egg Coat-Sperm Recognition at Fertilization.,Raj I, Sadat Al Hosseini H, Dioguardi E, Nishimura K, Han L, Villa A, de Sanctis D, Jovine L Cell. 2017 Jun 15;169(7):1315-1326.e17. doi: 10.1016/j.cell.2017.05.033. PMID:28622512<ref>PMID:28622512</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5ii6" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Dioguardi, E]] | |||
[[Category: Han, L]] | |||
[[Category: Jovine, L]] | |||
[[Category: Nishimura, K]] | |||
[[Category: Sanctis, D De]] | |||
[[Category: Cell adhesion]] | |||
[[Category: Egg coat]] | |||
[[Category: Egg-sperm interaction]] | |||
[[Category: Fertilization]] | |||
[[Category: Gamete recognition]] | |||
[[Category: Sperm receptor]] | |||
[[Category: Zona pellucida]] | |||
[[Category: Zp domain]] | |||
[[Category: Zp-n domain]] | |||
