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Structure paper

TitleStructures of Hsp90 alpha and Hsp90 beta bound to a purine-scaffold inhibitor reveal an exploitable residue for drug selectivity.
Journal, issue, pagesProteins, Vol. 87, Page 869-877, Year 2019
Publish dateNov 30, 2018 (structure data deposition date)
AuthorsHuck, J.D. / Que, N.L.S. / Sharma, S. / Taldone, T. / Chiosis, G. / Gewirth, D.T.
External linksProteins / PubMed:31141217
MethodsX-ray diffraction
Resolution1.43760580022 - 3.0922814017 Å
Structure data

PDB-6n8w:
Structure of Unliganded Hsp90-Beta N-Terminal Domain
Method: X-RAY DIFFRACTION / Resolution: 3.0922814017 Å

PDB-6n8x:
Hsp90-alpha bound to PU-11-trans
Method: X-RAY DIFFRACTION / Resolution: 1.49484474369 Å

PDB-6n8y:
Hsp90-beta bound to PU-11-trans
Method: X-RAY DIFFRACTION / Resolution: 1.55390799533 Å

PDB-6olx:
Hsp90-alpha S52A bound to PU-11-trans
Method: X-RAY DIFFRACTION / Resolution: 1.43760580022 Å

Chemicals

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

ChemComp-KFY:
9-[(2E)-but-2-en-1-yl]-8-[(3,4,5-trimethoxyphenyl)methyl]-9H-purin-6-amine

Source
  • homo sapiens (human)
KeywordsCHAPERONE / Heat-Shock / HSP90 / Cytosolic / chaperone/chaperone inhibitor / Inhibitor / Cancer / Cytosol / chaperone-chaperone inhibitor complex

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