View source for 3pry


==Crystal structure of the middle domain of human HSP90-beta refined at 2.3 A resolution==
<StructureSection load='3pry' size='340' side='right'caption='[[3pry]], [[Resolution|resolution]] 2.28&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3pry]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PRY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PRY 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]] 2.28&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <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=3pry FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pry OCA], [https://pdbe.org/3pry PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pry RCSB], [https://www.ebi.ac.uk/pdbsum/3pry PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pry ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HS90B_HUMAN HS90B_HUMAN] Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function.<ref>PMID:16478993</ref> <ref>PMID:19696785</ref> 

==See Also==
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Arrowsmith CH]]
[[Category: Ayinampudi V]]
[[Category: Berridge G]]
[[Category: Bountra C]]
[[Category: Bullock A]]
[[Category: Chaikuad A]]
[[Category: Che KH]]
[[Category: Cooper CDO]]
[[Category: Edwards A]]
[[Category: Fedorov O]]
[[Category: Keates T]]
[[Category: Krojer T]]
[[Category: Muniz JRC]]
[[Category: Phillips C]]
[[Category: Pilka E]]
[[Category: Sharpe TD]]
[[Category: Thangaratnarajah C]]
[[Category: Vollmar M]]
[[Category: Weigelt J]]
[[Category: Yue WW]]
[[Category: Zimmermann T]]
[[Category: Von Delft F]]