Structures of Hsp90α and Hsp90β bound to a purine-scaffold inhibitor reveal an exploitable residue for drug selectivity.


Journal

Proteins
ISSN: 1097-0134
Titre abrégé: Proteins
Pays: United States
ID NLM: 8700181

Informations de publication

Date de publication:
10 2019
Historique:
received: 09 01 2019
revised: 24 04 2019
accepted: 22 05 2019
pubmed: 30 5 2019
medline: 1 7 2020
entrez: 30 5 2019
Statut: ppublish

Résumé

Hsp90α and Hsp90β are implicated in a number of cancers and neurodegenerative disorders but the lack of selective pharmacological probes confounds efforts to identify their individual roles. Here, we analyzed the binding of an Hsp90α-selective PU compound, PU-11-trans, to the two cytosolic paralogs. We determined the co-crystal structures of Hsp90α and Hsp90β bound to PU-11-trans, as well as the structure of the apo Hsp90β NTD. The two inhibitor-bound structures reveal that Ser52, a nonconserved residue in the ATP binding pocket in Hsp90α, provides additional stability to PU-11-trans through a water-mediated hydrogen-bonding network. Mutation of Ser52 to alanine, as found in Hsp90β, alters the dissociation constant of Hsp90α for PU-11-trans to match that of Hsp90β. Our results provide a structural explanation for the binding preference of PU inhibitors for Hsp90α and demonstrate that the single nonconserved residue in the ATP-binding pocket may be exploited for α/β selectivity.

Identifiants

pubmed: 31141217
doi: 10.1002/prot.25750
pmc: PMC6718336
mid: NIHMS1530291
doi:

Substances chimiques

Amino Acids 0
HSP90 Heat-Shock Proteins 0
HSP90AA2P protein, human 0
HSP90AB1 protein, human 0
Purines 0

Types de publication

Journal Article Research Support, N.I.H., Extramural

Langues

eng

Sous-ensembles de citation

IM

Pagination

869-877

Subventions

Organisme : NCI NIH HHS
ID : P01-CA186866
Pays : United States
Organisme : NIA NIH HHS
ID : U01 AG032969
Pays : United States
Organisme : NCI NIH HHS
ID : R01 CA095130
Pays : United States
Organisme : NCI NIH HHS
ID : P50 CA192937
Pays : United States
Organisme : NCI NIH HHS
ID : R01 CA172546
Pays : United States
Organisme : NCI NIH HHS
ID : R01-CA095130
Pays : United States
Organisme : NCI NIH HHS
ID : P01 CA186866
Pays : United States
Organisme : NCI NIH HHS
ID : P30 CA008748
Pays : United States
Organisme : NIA NIH HHS
ID : R56 AG061869
Pays : United States

Informations de copyright

© 2019 Wiley Periodicals, Inc.

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Auteurs

John D Huck (JD)

Hauptman-Woodward Medical Research Institute, Buffalo, New York.
Department of Structural Biology, Jacobs School of Medicine & Biomedical Sciences, University at Buffalo, Buffalo, New York.

Nanette L S Que (NLS)

Hauptman-Woodward Medical Research Institute, Buffalo, New York.

Sahil Sharma (S)

Program in Chemical Biology and Department of Medicine, Memorial Sloan Kettering Cancer Center, New York, New York.

Tony Taldone (T)

Program in Chemical Biology and Department of Medicine, Memorial Sloan Kettering Cancer Center, New York, New York.

Gabriela Chiosis (G)

Program in Chemical Biology and Department of Medicine, Memorial Sloan Kettering Cancer Center, New York, New York.

Daniel T Gewirth (DT)

Hauptman-Woodward Medical Research Institute, Buffalo, New York.
Department of Structural Biology, Jacobs School of Medicine & Biomedical Sciences, University at Buffalo, Buffalo, New York.

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Classifications MeSH