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5ii6

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Crystal structure of the ZP-N1 domain of mouse sperm receptor ZP2 at 0.95 A resolution

Structural highlights

5ii6 is a 1 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 0.95Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5ii6"

@@ Line 1: / Line 1: @@
 ==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]] 0.95&Aring;' scene=''>
+<StructureSection load='5ii6' size='340' side='right'caption='[[5ii6]], [[Resolution|resolution]] 0.95&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5ii6]] is a 1 chain structure. 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]]</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]] 0.95&#8491;</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>
+<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>
 </table>
 == 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;">
 == Publication Abstract from PubMed ==
@@ Line 22: / Line 22: @@
 __TOC__
 </StructureSection>
-[[Category: Dioguardi, E]]
+[[Category: Large Structures]]
-[[Category: Han, L]]
+[[Category: Mus musculus]]
-[[Category: Jovine, L]]
+[[Category: De Sanctis D]]
-[[Category: Nishimura, K]]
+[[Category: Dioguardi E]]
-[[Category: Sanctis, D De]]
+[[Category: Han L]]
-[[Category: Cell adhesion]]
+[[Category: Jovine L]]
-[[Category: Egg coat]]
+[[Category: Nishimura K]]
-[[Category: Egg-sperm interaction]]
-[[Category: Fertilization]]
-[[Category: Gamete recognition]]
-[[Category: Sperm receptor]]
-[[Category: Zona pellucida]]
-[[Category: Zp domain]]
-[[Category: Zp-n domain]]

5ii6

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Current revision

Crystal structure of the ZP-N1 domain of mouse sperm receptor ZP2 at 0.95 A resolution

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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