ArticleScientific reports2015
A dynamic view of ATP-coupled functioning cycle of Hsp90 N-terminal domain.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 41 citations in OpenAlex.
- Distinct phosphorylation mechanisms as dynamic switches for Hsp90 regulation.Nature communications · 2026Article
- Combined Transcriptomic and Metabolomic Analyses of Low-Temperature Adaptation inInternational journal of molecular sciences · 2026Article
- Mechanism of client loading from BiP to Grp94 and its disruption by select inhibitors.Nature communications · 2025Article
- Site-specifically Phosphorylated Hsp90C-terminal Domain Variants Provide Access to Deciphering the Chaperone Code.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Structural Characterization of Heat Shock Protein 90β and Molecular Interactions with Geldanamycin and Ritonavir: A Computational Study.International journal of molecular sciences · 2024Article
- Hsp90 inhibition leads to an increase in surface expression of multiple immunological receptors in cancer cells.Frontiers in molecular biosciences · 2024Article
- Capsaicin binds the N-terminus of Hsp90, induces lysosomal degradation of Hsp70, and enhances the anti-tumor effects of 17-AAG (Tanespimycin).Scientific reports · 2023Article
- A hydrogen-deuterium exchange mass spectrometry-based protocol for protein-small molecule interaction analysis.Biophysics reports · 2023Article
- Visualizing the transiently populated closed-state of human HSP90 ATP binding domain.Nature communications · 2022Article
- Structure based design of effective HtpG-derived vaccine antigens againstFrontiers in molecular biosciences · 2022Article
- Inhibitors of theCells · 2021Review
- Induced fit versus conformational selection: From rate constants to fluxes… and back to rate constants.Pharmacology research & perspectives · 2021Article
- Allosteric Regulation of Hsp90α's Activity by Small Molecules Targeting the Middle Domain of the Chaperone.iScience · 2020Article
- Small-molecule inhibitor targeting the Hsp90-Cdc37 protein-protein interaction in colorectal cancer.Science advances · 2019Article
- Stimulation of heat shock protein 90 chaperone function through binding of a novobiocin analog KU-32.The Journal of biological chemistry · 2019Article
- Therapeutic Potential of the Hsp90/Cdc37 Interaction in Neurodegenerative Diseases.Frontiers in neuroscience · 2019Review
- Protein conformational flexibility modulates kinetics and thermodynamics of drug binding.Nature communications · 2017Article
- Molecular mechanism of bacterial Hsp90 pH-dependent ATPase activity.Protein science : a publication of the Protein Society · 2017Article
- Fluoride Alters Klk4 Expression in Maturation Ameloblasts through Androgen and Progesterone Receptor Signaling.Frontiers in physiology · 2017Article
- NMR-based platform for fragment-based lead discovery used in screening BRD4-targeted compounds.Acta pharmacologica Sinica · 2016Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Heat-shock protein 90 (Hsp90) is one of the most important chaperones involved in multiple cellular processes. The chaperoning function of Hsp90 is intimately coupled to the ATPase activity presented by its N-terminal domain. However, the molecular mechanism for the ATP-dependent working cycle of Hsp90 is still not fully understood. In this study, we use NMR techniques to investigate the structural characteristics and dynamic behaviors of Hsp90 N-terminal domain in its free and AMPPCP (ATP analogue) or ADP-bound states. We demonstrated that although AMPPCP and ADP bind to almost the same region of Hsp90, significantly different effects on the dynamics behaviors of the key structural elements were observed. AMPPCP binding favors the formation of the active homodimer of Hsp90 by enhancing the slow-motion featured conformational exchanges of those residues (A117-A141) within the lid segment (A111-G135) and around region, while ADP binding keeps Hsp90 staying at the inactive state by increasing the conformational rigidity of the lid segment and around region. Based on our findings, a dynamic working model for the ATP-dependent functioning cycle of Hsp90 was proposed.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.