View source for 3owd


==Crystal Structure of HSP90 with N-Aryl-benzimidazolone II==
<StructureSection load='3owd' size='340' side='right'caption='[[3owd]], [[Resolution|resolution]] 1.63&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3owd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OWD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OWD FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MEY:N-{[1-(5-CHLORO-2,4-DIHYDROXYPHENYL)-2-OXO-2,3-DIHYDRO-1H-BENZIMIDAZOL-5-YL]METHYL}NAPHTHALENE-1-SULFONAMIDE'>MEY</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3ow6|3ow6]], [[3owb|3owb]]</div></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HSP90AA1, HSP90A, HSPC1, HSPCA ([https://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'>[https://proteopedia.org/fgij/fg.htm?mol=3owd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3owd OCA], [https://pdbe.org/3owd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3owd RCSB], [https://www.ebi.ac.uk/pdbsum/3owd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3owd ProSAT]</span></td></tr>
</table>
== Function ==
[[https://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>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
We describe the development of a novel series of N-aryl-benzimidazolone HSP90 inhibitors (9) targeting the N-terminal ATP-ase site. SAR development was influenced by structure-based design based around X-ray structures of ligand bound HSP90 complexes. Lead compounds exhibited high binding affinities, ATP-ase inhibition and cellular client protein degradation.

N-aryl-benzimidazolones as novel small molecule HSP90 inhibitors.,Bruncko M, Tahir SK, Song X, Chen J, Ding H, Huth JR, Jin S, Judge RA, Madar DJ, Park CH, Park CM, Petros AM, Tse C, Rosenberg SH, Elmore SW Bioorg Med Chem Lett. 2010 Dec 15;20(24):7503-6. Epub 2010 Oct 12. PMID:21106457<ref>PMID:21106457</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3owd" style="background-color:#fffaf0;"></div>

==See Also==
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Human]]
[[Category: Large Structures]]
[[Category: Park, C H]]
[[Category: Chaperone]]
[[Category: Hsp90]]