Exhaustive search of the configurational space of heat-shock protein 90 with its inhibitor by multicanonical molecular dynamics based dynamic docking.

dynamic docking enhanced conformational sampling free energy landscape heat-shock protein 90 multicanonical Molecular Dynamics

Journal

Journal of computational chemistry
ISSN: 1096-987X
Titre abrégé: J Comput Chem
Pays: United States
ID NLM: 9878362

Informations de publication

Date de publication:
30 06 2020
Historique:
received: 25 01 2020
revised: 18 03 2020
accepted: 25 03 2020
pubmed: 9 4 2020
medline: 25 6 2021
entrez: 9 4 2020
Statut: ppublish

Résumé

Multicanonical molecular dynamics based dynamic docking was used to exhaustively search the configurational space of an inhibitor binding to the N-terminal domain of heat-shock protein 90 (Hsp90). The obtained structures at 300 K cover a wide structural ensemble, with the top two clusters ranked by their free energy coinciding with the native binding site. The representative structure of the most stable cluster reproduced the experimental binding configuration, but an interesting conformational change in Hsp90 could be observed. The combined effects of solvation and ligand binding shift the equilibrium from a preferred loop-in conformation in the unbound state to an α-helical one in the bound state for the flexible lid region of Hsp90. Thus, our dynamic docking method is effective at predicting the native binding site while exhaustively sampling a wide configurational space, modulating the protein structure upon binding.

Identifiants

pubmed: 32267975
doi: 10.1002/jcc.26203
doi:

Substances chimiques

HSP90 Heat-Shock Proteins 0
Ligands 0

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

1606-1615

Informations de copyright

© 2020 Wiley Periodicals, Inc.

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Auteurs

Gert-Jan Bekker (GJ)

Institute for Protein Research, Osaka University, Osaka, Japan.

Mitsugu Araki (M)

Graduate School of Medicine, Kyoto University, Kyoto, Japan.

Kanji Oshima (K)

Biotechnology Research Laboratories, Kaneka Corporation, Takasago, Hyogo, Japan.

Yasushi Okuno (Y)

Graduate School of Medicine, Kyoto University, Kyoto, Japan.

Narutoshi Kamiya (N)

Graduate School of Simulation Studies, University of Hyogo, Kobe, Hyogo, Japan.

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