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| | <StructureSection load='3nk3' size='340' side='right'caption='[[3nk3]], [[Resolution|resolution]] 2.60Å' scene=''> | | <StructureSection load='3nk3' size='340' side='right'caption='[[3nk3]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3nk3]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Chick Chick]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NK3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NK3 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3nk3]] 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=3NK3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NK3 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=A2G:N-ACETYL-2-DEOXY-2-AMINO-GALACTOSE'>A2G</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3d4c|3d4c]], [[3d4g|3d4g]], [[3ef7|3ef7]], [[3nk4|3nk4]]</div></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>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=PRD_900084:Thomsen-Friedenreich+antigen'>PRD_900084</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=3nk3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nk3 OCA], [https://pdbe.org/3nk3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nk3 RCSB], [https://www.ebi.ac.uk/pdbsum/3nk3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nk3 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=3nk3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nk3 OCA], [https://pdbe.org/3nk3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nk3 RCSB], [https://www.ebi.ac.uk/pdbsum/3nk3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nk3 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>
| + | [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: Chick]] | + | [[Category: Gallus gallus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Jovine, L]] | + | [[Category: Jovine L]] |
| - | [[Category: Monne, M]] | + | [[Category: Monne M]] |
| - | [[Category: Biodiversity]]
| + | |
| - | [[Category: Cell adhesion]]
| + | |
| - | [[Category: Core-1]]
| + | |
| - | [[Category: Egg coat]]
| + | |
| - | [[Category: Egg-sperm interaction]]
| + | |
| - | [[Category: Ehp]]
| + | |
| - | [[Category: External hydrophobic patch]]
| + | |
| - | [[Category: Extracellular matrix]]
| + | |
| - | [[Category: Fertilization]]
| + | |
| - | [[Category: Glycoprotein]]
| + | |
| - | [[Category: Ihp]]
| + | |
| - | [[Category: Immunoglobulin-like fold]]
| + | |
| - | [[Category: Infertility]]
| + | |
| - | [[Category: Internal hydrophobic patch]]
| + | |
| - | [[Category: O-linked carbohydrate]]
| + | |
| - | [[Category: Oocyte]]
| + | |
| - | [[Category: Receptor]]
| + | |
| - | [[Category: Secreted]]
| + | |
| - | [[Category: Speciation]]
| + | |
| - | [[Category: Species-specific gamete recognition]]
| + | |
| - | [[Category: Sperm-combining site]]
| + | |
| - | [[Category: T-antigen]]
| + | |
| - | [[Category: Transmembrane]]
| + | |
| - | [[Category: Vitelline envelope]]
| + | |
| - | [[Category: Zona pellucida]]
| + | |
| - | [[Category: Zp domain]]
| + | |
| - | [[Category: Zp module]]
| + | |
| Structural highlights
Function
ZP3_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 PubMed
ZP3, 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
- ↑ Bausek N, Ruckenbauer HH, Pfeifer S, Schneider WJ, Wohlrab F. Interaction of sperm with purified native chicken ZP1 and ZPC proteins. Biol Reprod. 2004 Aug;71(2):684-90. Epub 2004 Apr 28. PMID:15115720 doi:10.1095/biolreprod.104.028605
- ↑ Han L, Monne M, Okumura H, Schwend T, Cherry AL, Flot D, Matsuda T, Jovine L. Insights into egg coat assembly and egg-sperm interaction from the X-ray structure of full-length ZP3. Cell. 2010 Oct 29;143(3):404-15. Epub 2010 Oct 21. PMID:20970175 doi:10.1016/j.cell.2010.09.041
- ↑ Han L, Monne M, Okumura H, Schwend T, Cherry AL, Flot D, Matsuda T, Jovine L. Insights into egg coat assembly and egg-sperm interaction from the X-ray structure of full-length ZP3. Cell. 2010 Oct 29;143(3):404-15. Epub 2010 Oct 21. PMID:20970175 doi:10.1016/j.cell.2010.09.041
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