5lr7
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==CRYSTAL STRUCTURE OF HSP90 IN COMPLEX WITH SAR567530== | |
| - | + | <StructureSection load='5lr7' size='340' side='right' caption='[[5lr7]], [[Resolution|resolution]] 1.86Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[5lr7]] 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=5LR7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LR7 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=73J:~{N}-[(9~{R})-4-(5-fluoranyl-1~{H}-benzimidazol-2-yl)-9~{H}-fluoren-9-yl]-1~{H}-pyrrolo[2,3-b]pyridine-4-carboxamide'>73J</scene></td></tr> | |
| - | [[Category: | + | <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> |
| - | [[Category: | + | <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=5lr7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lr7 OCA], [http://pdbe.org/5lr7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lr7 RCSB], [http://www.ebi.ac.uk/pdbsum/5lr7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lr7 ProSAT]</span></td></tr> |
| - | [[Category: | + | </table> |
| + | == Function == | ||
| + | [[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> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Human]] | ||
| + | [[Category: DUPUY, A]] | ||
| + | [[Category: VALLEE, F]] | ||
| + | [[Category: Chaperone protein]] | ||
Revision as of 20:56, 15 November 2017
CRYSTAL STRUCTURE OF HSP90 IN COMPLEX WITH SAR567530
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