View source for 6gf6


==Molecular basis of egg coat filament cross-linking: high-resolution structure of the partially deglycosylated ZP1 ZP-N1 domain homodimer==
<StructureSection load='6gf6' size='340' side='right'caption='[[6gf6]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6gf6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GF6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6GF6 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=6gf6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gf6 OCA], [https://pdbe.org/6gf6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6gf6 RCSB], [https://www.ebi.ac.uk/pdbsum/6gf6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6gf6 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A140JXP0_CHICK A0A140JXP0_CHICK] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Mammalian fertilisation begins when sperm interacts with the egg zona pellucida (ZP), whose ZP1 subunit is important for fertility by covalently cross-linking ZP filaments into a three-dimensional matrix. Like ZP4, a structurally-related component absent in the mouse, ZP1 is predicted to contain an N-terminal ZP-N domain of unknown function. Here we report a characterisation of ZP1 proteins carrying mutations from infertile patients, which suggests that, in human, filament cross-linking by ZP1 is crucial to form a stable ZP. We map the function of ZP1 to its ZP-N1 domain and determine crystal structures of ZP-N1 homodimers from a chicken homolog of ZP1. These reveal that ZP filament cross-linking is highly plastic and can be modulated by ZP1 fucosylation and, potentially, zinc sparks. Moreover, we show that ZP4 ZP-N1 forms non-covalent homodimers in chicken but not in human. Together, these data identify human ZP1 cross-links as a promising target for non-hormonal contraception.

Molecular basis of egg coat cross-linking sheds light on ZP1-associated female infertility.,Nishimura K, Dioguardi E, Nishio S, Villa A, Han L, Matsuda T, Jovine L Nat Commun. 2019 Jul 12;10(1):3086. doi: 10.1038/s41467-019-10931-5. PMID:31300655<ref>PMID:31300655</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6gf6" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Gallus gallus]]
[[Category: Large Structures]]
[[Category: Jovine L]]
[[Category: Nishimura K]]