6gf7: Difference between revisions
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==Molecular basis of egg coat filament cross-linking: Zn-SAD structure of the partially deglycosylated ZP1 ZP-N1 domain homodimer== | |||
<StructureSection load='6gf7' size='340' side='right'caption='[[6gf7]], [[Resolution|resolution]] 2.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6gf7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Chick Chick]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GF7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6GF7 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6gf6|6gf6]], [[6gf8|6gf8]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ZP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9031 CHICK])</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=6gf7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gf7 OCA], [http://pdbe.org/6gf7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6gf7 RCSB], [http://www.ebi.ac.uk/pdbsum/6gf7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6gf7 ProSAT]</span></td></tr> | |||
</table> | |||
<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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6gf7" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Chick]] | |||
[[Category: Large Structures]] | |||
[[Category: Jovine, L]] | |||
[[Category: Nishimura, K]] | |||
[[Category: Cell adhesion]] | |||
[[Category: Egg coat filament cross-linking]] | |||
[[Category: Egg coat penetration by sperm]] | |||
[[Category: Zona pellucida]] | |||
[[Category: Zp domain]] | |||
[[Category: Zp module]] | |||
[[Category: Zp-n domain]] | |||
[[Category: Zp1]] | |||
