6aol
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of molecular chaperone Grp94 bound to selective inhibitor methyl 3-chloro-2-(2-{2-[(4-fluorophenyl)methyl]phenyl}ethyl)-4,6-dihydroxybenzoate== | |
| + | <StructureSection load='6aol' size='340' side='right' caption='[[6aol]], [[Resolution|resolution]] 2.76Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6aol]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AOL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6AOL FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=P33:3,6,9,12,15,18-HEXAOXAICOSANE-1,20-DIOL'>P33</scene>, <scene name='pdbligand=VC1:methyl+3-chloro-2-(2-{2-[(4-fluorophenyl)methyl]phenyl}ethyl)-4,6-dihydroxybenzoate'>VC1</scene></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=6aol FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6aol OCA], [http://pdbe.org/6aol PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6aol RCSB], [http://www.ebi.ac.uk/pdbsum/6aol PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6aol ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/ENPL_CANLF ENPL_CANLF]] Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors. Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity (By similarity). | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Glucose regulated protein 94 (Grp94) is the endoplasmic reticulum (ER) resident isoform of the 90 kDa heat shock protein (Hsp90) family and its inhibition represents a promising therapeutic target for the treatment of many diseases. Modification of the first generation cis-amide bioisostere imidazole to alter the angle between the resorcinol ring and the benzyl side chain via cis-amide replacements produced compounds with improved Grp94 affinity and selectivity. Structure-activity relationship studies led to the discovery of compound 30, which exhibits 540 nm affinity and 73-fold selectivity towards Grp94. Grp94 is responsible for the maturation and trafficking of proteins associated with cell signaling and motility, including select integrins. The Grp94-selective inhibitor 30 was shown to exhibit potent anti-migratory effects against multiple aggressive and metastatic cancers. | ||
| - | + | Second Generation Grp94-Selective Inhibitors Provide Opportunities for the Inhibition of Metastatic Cancer.,Crowley VM, Huard DJE, Lieberman RL, Blagg BSJ Chemistry. 2017 Aug 30. doi: 10.1002/chem.201703398. PMID:28857290<ref>PMID:28857290</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6aol" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Huard, D J.E]] | ||
| + | [[Category: Lieberman, R L]] | ||
| + | [[Category: Chaperone-inhibitor complex]] | ||
| + | [[Category: Grp94]] | ||
| + | [[Category: Hsp90]] | ||
Revision as of 06:54, 11 October 2017
Structure of molecular chaperone Grp94 bound to selective inhibitor methyl 3-chloro-2-(2-{2-[(4-fluorophenyl)methyl]phenyl}ethyl)-4,6-dihydroxybenzoate
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