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Structure paper

TitleDipyridamole interacts with the N-terminal domain of HSP90 and antagonizes the function of the chaperone in multiple cancer cell lines.
Journal, issue, pagesBiochem Pharmacol, Vol. 207, Page 115376-115376, Year 2022
Publish dateDec 3, 2020 (structure data deposition date)
AuthorsGao, J. / Zhou, C. / Zhong, Y. / Shi, L. / Luo, X. / Su, H. / Li, M. / Xu, Y. / Zhang, N. / Zhou, H.
External linksBiochem Pharmacol / PubMed:36513142
MethodsX-ray diffraction
Resolution2.34 Å
Structure data

PDB-7dmc:
Dipyridamole binds to the N-terminal domain of human Hsp90A
Method: X-RAY DIFFRACTION / Resolution: 2.34 Å

Chemicals

ChemComp-H9F:
2-[[2-[bis(2-hydroxyethyl)amino]-4,8-di(piperidin-1-yl)pyrimido[5,4-d]pyrimidin-6-yl]-(2-hydroxyethyl)amino]ethanol / inhibitor*YM

ChemComp-CL:
Unknown entry

ChemComp-MG:
Unknown entry

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsCHAPERONE / ATP binding domain / Hsp90 / Dipyridamole

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