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| | ==Crystal structure of the ZP-N1 domain of mouse sperm receptor ZP2 at 0.95 A resolution== | | ==Crystal structure of the ZP-N1 domain of mouse sperm receptor ZP2 at 0.95 A resolution== |
| - | <StructureSection load='5ii6' size='340' side='right' caption='[[5ii6]], [[Resolution|resolution]] 0.95Å' scene=''> | + | <StructureSection load='5ii6' size='340' side='right'caption='[[5ii6]], [[Resolution|resolution]] 0.95Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5ii6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5II6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5II6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5ii6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5II6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5II6 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3d4c|3d4c]], [[3d4g|3d4g]], [[3ef7|3ef7]], [[3nk3|3nk3]], [[3nk4|3nk4]], [[5bup|5bup]], [[5ii5|5ii5]], [[5ii4|5ii4]], [[5iic|5iic]]</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]] 0.95Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Zp2, Zp-2, Zpa ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=5ii6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ii6 OCA], [https://pdbe.org/5ii6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ii6 RCSB], [https://www.ebi.ac.uk/pdbsum/5ii6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ii6 ProSAT]</span></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=5ii6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ii6 OCA], [http://pdbe.org/5ii6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ii6 RCSB], [http://www.ebi.ac.uk/pdbsum/5ii6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ii6 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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> | + | [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> |
| | <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: Lk3 transgenic mice]] | + | [[Category: Large Structures]] |
| - | [[Category: Dioguardi, E]] | + | [[Category: Mus musculus]] |
| - | [[Category: Han, L]]
| + | [[Category: De Sanctis D]] |
| - | [[Category: Jovine, L]]
| + | [[Category: Dioguardi E]] |
| - | [[Category: Nishimura, K]]
| + | [[Category: Han L]] |
| - | [[Category: Sanctis, D De]] | + | [[Category: Jovine L]] |
| - | [[Category: Cell adhesion]] | + | [[Category: Nishimura K]] |
| - | [[Category: Egg coat]] | + | |
| - | [[Category: Egg-sperm interaction]] | + | |
| - | [[Category: Fertilization]] | + | |
| - | [[Category: Gamete recognition]]
| + | |
| - | [[Category: Sperm receptor]]
| + | |
| - | [[Category: Zona pellucida]]
| + | |
| - | [[Category: Zp domain]]
| + | |
| - | [[Category: Zp-n domain]]
| + | |
| Structural highlights
Function
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.[1]
Publication Abstract from PubMed
Recognition between sperm and the egg surface marks the beginning of life in all sexually reproducing organisms. This fundamental biological event depends on the species-specific interaction between rapidly evolving counterpart molecules on the gametes. We report biochemical, crystallographic, and mutational studies of domain repeats 1-3 of invertebrate egg coat protein VERL and their interaction with cognate sperm protein lysin. VERL repeats fold like the functionally essential N-terminal repeat of mammalian sperm receptor ZP2, whose structure is also described here. Whereas sequence-divergent repeat 1 does not bind lysin, repeat 3 binds it non-species specifically via a high-affinity, largely hydrophobic interface. Due to its intermediate binding affinity, repeat 2 selectively interacts with lysin from the same species. Exposure of a highly positively charged surface of VERL-bound lysin suggests that complex formation both disrupts the organization of egg coat filaments and triggers their electrostatic repulsion, thereby opening a hole for sperm penetration and fusion.
Structural Basis of Egg Coat-Sperm Recognition at Fertilization.,Raj I, Sadat Al Hosseini H, Dioguardi E, Nishimura K, Han L, Villa A, de Sanctis D, Jovine L Cell. 2017 Jun 15;169(7):1315-1326.e17. doi: 10.1016/j.cell.2017.05.033. PMID:28622512[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Burkart AD, Xiong B, Baibakov B, Jimenez-Movilla M, Dean J. Ovastacin, a cortical granule protease, cleaves ZP2 in the zona pellucida to prevent polyspermy. J Cell Biol. 2012 Apr 2;197(1):37-44. doi: 10.1083/jcb.201112094. PMID:22472438 doi:http://dx.doi.org/10.1083/jcb.201112094
- ↑ Raj I, Sadat Al Hosseini H, Dioguardi E, Nishimura K, Han L, Villa A, de Sanctis D, Jovine L. Structural Basis of Egg Coat-Sperm Recognition at Fertilization. Cell. 2017 Jun 15;169(7):1315-1326.e17. doi: 10.1016/j.cell.2017.05.033. PMID:28622512 doi:http://dx.doi.org/10.1016/j.cell.2017.05.033
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