5lq9
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==CRYSTAL STRUCTURE OF HSP90 IN COMPLEX WITH SAR200323.== | |
| - | + | <StructureSection load='5lq9' size='340' side='right' caption='[[5lq9]], [[Resolution|resolution]] 1.90Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[5lq9]] 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=5LQ9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LQ9 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=72K:4-(3-methyl-4-quinolin-3-yl-indazol-1-yl)-2-[(4-oxidanylcyclohexyl)amino]benzamide'>72K</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> |
| + | <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=5lq9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lq9 OCA], [http://pdbe.org/5lq9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lq9 RCSB], [http://www.ebi.ac.uk/pdbsum/5lq9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lq9 ProSAT]</span></td></tr> | ||
| + | </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: Dupuy, A]] | ||
[[Category: Vallee, F]] | [[Category: Vallee, F]] | ||
| + | [[Category: Chaperone protein]] | ||
Revision as of 20:56, 15 November 2017
CRYSTAL STRUCTURE OF HSP90 IN COMPLEX WITH SAR200323.
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