View source for 5ds2


==Core domain of the class I small heat-shock protein HSP 18.1 from Pisum sativum==
<StructureSection load='5ds2' size='340' side='right'caption='[[5ds2]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5ds2]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DS2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DS2 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=5ds2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ds2 OCA], [https://pdbe.org/5ds2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ds2 RCSB], [https://www.ebi.ac.uk/pdbsum/5ds2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ds2 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HSP11_PEA HSP11_PEA] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Oligomeric proteins assemble with exceptional selectivity, even in the presence of closely related proteins, to perform their cellular roles. We show that most proteins related by gene duplication of an oligomeric ancestor have evolved to avoid hetero-oligomerization and that this correlates with their acquisition of distinct functions. We report how coassembly is avoided by two oligomeric small heat-shock protein paralogs. A hierarchy of assembly, involving intermediates that are populated only fleetingly at equilibrium, ensures selective oligomerization. Conformational flexibility at noninterfacial regions in the monomers prevents coassembly, allowing interfaces to remain largely conserved. Homomeric oligomers must overcome the entropic benefit of coassembly and, accordingly, homomeric paralogs comprise fewer subunits than homomers that have no paralogs.

Structural principles that enable oligomeric small heat-shock protein paralogs to evolve distinct functions.,Hochberg GKA, Shepherd DA, Marklund EG, Santhanagoplan I, Degiacomi MT, Laganowsky A, Allison TM, Basha E, Marty MT, Galpin MR, Struwe WB, Baldwin AJ, Vierling E, Benesch JLP Science. 2018 Feb 23;359(6378):930-935. doi: 10.1126/science.aam7229. PMID:29472485<ref>PMID:29472485</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5ds2" style="background-color:#fffaf0;"></div>

==See Also==
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pisum sativum]]
[[Category: Allison TM]]
[[Category: Benesch JLP]]
[[Category: Hochberg GKA]]
[[Category: Laganowsky A]]
[[Category: Shepherd DA]]