5t21

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m (Protected "5t21" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 5t21 is ON HOLD
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==CRYSTAL STRUCTURE OF HSP90 IN COMPLEX WITH SAR148019.==
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<StructureSection load='5t21' size='340' side='right' caption='[[5t21]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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Authors: Vallee, F., Dupuy, A.
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5t21]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5T21 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5T21 FirstGlance]. <br>
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Description: CRYSTAL STRUCTURE OF HSP90 IN COMPLEX WITH SAR148019.
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=74E:2-[(4-oxidanylcyclohexyl)amino]-4-(3,6,6-trimethyl-4-oxidanylidene-5,7-dihydroindol-1-yl)benzamide'>74E</scene></td></tr>
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[[Category: Unreleased Structures]]
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HSP90AA1, HSP90A, HSPC1, HSPCA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<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=5t21 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t21 OCA], [http://pdbe.org/5t21 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5t21 RCSB], [http://www.ebi.ac.uk/pdbsum/5t21 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5t21 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/HS90A_HUMAN HS90A_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:15937123</ref> <ref>PMID:11274138</ref>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Human]]
[[Category: Dupuy, A]]
[[Category: Dupuy, A]]
[[Category: Vallee, F]]
[[Category: Vallee, F]]
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[[Category: Chaperone protein]]

Revision as of 21:02, 15 November 2017

CRYSTAL STRUCTURE OF HSP90 IN COMPLEX WITH SAR148019.

5t21, resolution 2.10Å

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