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TitleIdentification of a new series of potent diphenol HSP90 inhibitors by fragment merging and structure-based optimization
Journal, issue, pagesBioorg. Med. Chem. Lett., Vol. 24, Page 2525-2529, Year 2014
Publish dateJun 18, 2013 (structure data deposition date)
AuthorsRen, J. / Li, J. / Wang, Y. / Chen, W. / Shen, A. / Liu, H. / Chen, D. / Cao, D. / Li, Y. / Zhang, N. ...Ren, J. / Li, J. / Wang, Y. / Chen, W. / Shen, A. / Liu, H. / Chen, D. / Cao, D. / Li, Y. / Zhang, N. / Xu, Y. / Geng, M. / He, J. / Xiong, B. / Shen, J.
External linksBioorg. Med. Chem. Lett. / PubMed:24751441
MethodsX-ray diffraction
Resolution1.649 - 1.75 Å
Structure data

PDB-4l8z:
Crystal structure of Human Hsp90 with RL1
Method: X-RAY DIFFRACTION / Resolution: 1.703 Å

PDB-4l91:
Crystal structure of Human Hsp90 with X29
Method: X-RAY DIFFRACTION / Resolution: 1.75 Å

PDB-4l94:
Crystal structure of Human Hsp90 with S46
Method: X-RAY DIFFRACTION / Resolution: 1.649 Å

Chemicals

ChemComp-RL1:
[5-(6-bromo[1,2,4]triazolo[4,3-a]pyridin-3-yl)-2,4-dihydroxyphenyl](3,4-dihydroisoquinolin-2(1H)-yl)methanone

ChemComp-HOH:
WATER

ChemComp-X29:
4-(6-bromo[1,2,4]triazolo[4,3-a]pyridin-3-yl)-6-chlorobenzene-1,3-diol

ChemComp-S46:
(4-hydroxyphenyl)(4-methylpiperazin-1-yl)methanone

Source
  • homo sapiens (human)
KeywordsChaperone/Chaperone Inhibitor / ATP hydrolysis / Hsp90N-Hsp90N Inhibitor complex / Chaperone-Chaperone Inhibitor complex

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