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8rkh

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Current revision (09:53, 17 October 2024) (edit) (undo)
 
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8rkh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8rkh OCA], [https://pdbe.org/8rkh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8rkh RCSB], [https://www.ebi.ac.uk/pdbsum/8rkh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8rkh ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8rkh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8rkh OCA], [https://pdbe.org/8rkh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8rkh RCSB], [https://www.ebi.ac.uk/pdbsum/8rkh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8rkh ProSAT]</span></td></tr>
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</table>
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== Function ==
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<div style="background-color:#fffaf0;">
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[https://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>
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== Publication Abstract from PubMed ==
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Following the fertilization of an egg by a single sperm, the egg coat or zona pellucida (ZP) hardens and polyspermy is irreversibly blocked. These events are associated with the cleavage of the N-terminal region (NTR) of glycoprotein ZP2, a major subunit of ZP filaments. ZP2 processing is thought to inactivate sperm binding to the ZP, but its molecular consequences and connection with ZP hardening are unknown. Biochemical and structural studies show that cleavage of ZP2 triggers its oligomerization. Moreover, the structure of a native vertebrate egg coat filament, combined with AlphaFold predictions of human ZP polymers, reveals that two protofilaments consisting of type I (ZP3) and type II (ZP1/ZP2/ZP4) components interlock into a left-handed double helix from which the NTRs of type II subunits protrude. Together, these data suggest that oligomerization of cleaved ZP2 NTRs extensively cross-links ZP filaments, rigidifying the egg coat and making it physically impenetrable to sperm.
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ZP2 cleavage blocks polyspermy by modulating the architecture of the egg coat.,Nishio S, Emori C, Wiseman B, Fahrenkamp D, Dioguardi E, Zamora-Caballero S, Bokhove M, Han L, Stsiapanava A, Algarra B, Lu Y, Kodani M, Bainbridge RE, Komondor KM, Carlson AE, Landreh M, de Sanctis D, Yasumasu S, Ikawa M, Jovine L Cell. 2024 Mar 14;187(6):1440-1459.e24. doi: 10.1016/j.cell.2024.02.013. PMID:38490181<ref>PMID:38490181</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 8rkh" style="background-color:#fffaf0;"></div>
== References ==
== References ==
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Current revision

Crystal structure of the ZP-N2 and ZP-N3 domains of mouse ZP2 (mZP2-N2N3)

PDB ID 8rkh

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