3nk4: Difference between revisions
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==Crystal structure of full-length sperm receptor ZP3 at 2.0 A resolution== | ==Crystal structure of full-length sperm receptor ZP3 at 2.0 A resolution== | ||
<StructureSection load='3nk4' size='340' side='right' caption='[[3nk4]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='3nk4' size='340' side='right'caption='[[3nk4]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3nk4]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3nk4]] is a 4 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=3NK4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NK4 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=A2G:N-ACETYL-2-DEOXY-2-AMINO-GALACTOSE'>A2G</scene>, <scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A2G:N-ACETYL-2-DEOXY-2-AMINO-GALACTOSE'>A2G</scene>, <scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3nk4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nk4 OCA], [https://pdbe.org/3nk4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nk4 RCSB], [https://www.ebi.ac.uk/pdbsum/3nk4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nk4 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/ZP3_CHICK ZP3_CHICK] Component of the zona pellucida, which mediates species-specific sperm binding. Directly binds to sperm. Important for egg fertilization.<ref>PMID:15115720</ref> <ref>PMID:20970175</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Gallus gallus]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Jovine L]] | ||
[[Category: | [[Category: Monne M]] | ||
Latest revision as of 12:16, 6 September 2023
Crystal structure of full-length sperm receptor ZP3 at 2.0 A resolutionCrystal structure of full-length sperm receptor ZP3 at 2.0 A resolution
Structural highlights
FunctionZP3_CHICK Component of the zona pellucida, which mediates species-specific sperm binding. Directly binds to sperm. Important for egg fertilization.[1] [2] Publication Abstract from PubMedZP3, a major component of the zona pellucida (ZP) matrix coating mammalian eggs, is essential for fertilization by acting as sperm receptor. By retaining a propeptide that contains a polymerization-blocking external hydrophobic patch (EHP), we determined the crystal structure of an avian homolog of ZP3 at 2.0 A resolution. The structure unveils the fold of a complete ZP domain module in a homodimeric arrangement required for secretion and reveals how EHP prevents premature incorporation of ZP3 into the ZP. This suggests mechanisms underlying polymerization and how local structural differences, reflected by alternative disulfide patterns, control the specificity of ZP subunit interaction. Close relative positioning of a conserved O-glycan important for sperm binding and the hypervariable, positively selected C-terminal region of ZP3 suggests a concerted role in the regulation of species-restricted gamete recognition. Alternative conformations of the area around the O-glycan indicate how sperm binding could trigger downstream events via intramolecular signaling. Insights into egg coat assembly and egg-sperm interaction from the X-ray structure of full-length ZP3.,Han L, Monne M, Okumura H, Schwend T, Cherry AL, Flot D, Matsuda T, Jovine L Cell. 2010 Oct 29;143(3):404-15. Epub 2010 Oct 21. PMID:20970175[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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