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Structure paper

TitleAccurate Characterization of Binding Kinetics and Allosteric Mechanisms for the HSP90 Chaperone Inhibitors Using AI-Augmented Integrative Biophysical Studies.
Journal, issue, pagesJacs Au, Vol. 4, Page 1632-1645, Year 2024
Publish dateAug 22, 2023 (structure data deposition date)
AuthorsXu, C. / Zhang, X. / Zhao, L. / Verkhivker, G.M. / Bai, F.
External linksJacs Au / PubMed:38665669
MethodsX-ray diffraction
Resolution1.55 - 2.25 Å
Structure data

PDB-8ki4:
Crystal structure of human HSP90 in intermediate state
Method: X-RAY DIFFRACTION / Resolution: 1.55 Å

PDB-8w4v:
Crystal structure of human HSP90 in complex with compound 4
Method: X-RAY DIFFRACTION / Resolution: 1.81 Å

PDB-8w8k:
Crystal structures of HSP90 and the compound Ganetespid in the "closed" conformation
Method: X-RAY DIFFRACTION / Resolution: 2.25 Å

Chemicals

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-HOH:
WATER

ChemComp-MG:
Unknown entry


ChemComp, No image

ChemComp-Q9O:
Unknown entry

ChemComp-TUH:
5-[2,4-dihydroxy-5-(propan-2-yl)phenyl]-4-(1-methyl-1H-indol-5-yl)-2,4-dihydro-3H-1,2,4-triazol-3-one

Source
  • homo sapiens (human)
KeywordsCHAPERONE / HSP90 / ATPase / NTD / Complex / Inhibitor

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