5mr2: Difference between revisions

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'''Unreleased structure'''


The entry 5mr2 is ON HOLD  until Paper Publication
==Crystal structure of red abalone VERL repeat 2 with linker at 2.5 A resolution==
<StructureSection load='5mr2' size='340' side='right' caption='[[5mr2]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5mr2]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MR2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5MR2 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></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ii4|5ii4]], [[5ii5|5ii5]], [[5ii6|5ii6]], [[5iia|5iia]], [[5iib|5iib]], [[3d4c|3d4c]], [[3d4g|3d4g]], [[3ef7|3ef7]], [[3nk3|3nk3]], [[3nk4|3nk4]]</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=5mr2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mr2 OCA], [http://pdbe.org/5mr2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5mr2 RCSB], [http://www.ebi.ac.uk/pdbsum/5mr2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5mr2 ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== 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.


Authors:  
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<ref>PMID:28622512</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 5mr2" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Al-Hosseini, H Sadat]]
[[Category: Jovine, L]]
[[Category: Nishimura, K]]
[[Category: Raj, I]]
[[Category: Sanctis, D De]]
[[Category: Cell adhesion]]
[[Category: Egg-sperm interaction]]
[[Category: Fertilization]]
[[Category: Gamete recognition]]
[[Category: Sperm receptor]]
[[Category: Vitelline envelope]]

Revision as of 10:51, 3 August 2017

Crystal structure of red abalone VERL repeat 2 with linker at 2.5 A resolution

5mr2, resolution 2.50Å

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