Structure and in vivo function of Hsp90

Pearl, Laurence H; Prodromou, Chrisostomos

doi:10.1016/s0959-440x(99)00047-0

Cited by 326Heat shock proteins researchProtein Structure and DynamicsUbiquitin and proteasome pathways

Structure and in vivo function of Hsp90

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Pearl, Laurence H, Prodromou, Chrisostomos·2000·Current Opinion in Structural Biology

DOI 10.1016/s0959-440x(99)00047-0

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Abstract

Until recently, Hsp90 was one of the least well understood of the molecular chaperones, but considerable progress is now being made in unravelling its biochemistry. Hsp90 has now been shown to possess an inherent ATPase that is essential for the activation of authentic 'client' proteins in vivo and in vitro. The molecular detail of Hsp90's interactions with co-chaperones is also becoming clearer and the identification of key roles in assembling regulatory and signalling pathways has made it a target for anticancer drug development. Despite this, a clear understanding of how Hsp90 contributes to the folding and/or activation of its client proteins remains some way off.

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The Hsp90 protein has three domains and operates as a dimer.
“Briefly, the Hsp90 protein has three domains and operates as a dimer24-26 (Figure 1).”
From Fungal Hsp90: a biological transistor that tunes cellular outputs to thermal inputs (2012) · cites this paper as [24]
Hsp90 has weak intrinsic ATPase activity that is modulated by interactions with client proteins and co-chaperones.
“Hsp90 has weak intrinsic ATPase activity that is modulated by interactions with client proteins and co-chaperones.”
From Fungal Hsp90: a biological transistor that tunes cellular outputs to thermal inputs (2012) · cites this paper as [24]
The flexible Hsp90 dimer undergoes major conformational shifts during a dynamic chaperone cycle that is driven by ATP hydrolysis.
“The flexible Hsp90 dimer undergoes major conformational shifts during a dynamic chaperone cycle that is driven by ATP hydrolysis17,23-26 (Figure 1).”
From Fungal Hsp90: a biological transistor that tunes cellular outputs to thermal inputs (2012) · cites this paper as [24]

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Authors: Pearl, L. H., & Prodromou, C.
Affiliations: Institute of Cancer Research (GB)
Corresponding author: Pearl, Laurence H
ORCID: Pearl, Laurence H
Prodromou, Chrisostomos
Venue: Current Opinion in Structural Biology
Publisher: Elsevier BV
Published: 2000-02
Volume: 10
Issue: 1
Pages: 46-51
ISSN: 0959-440X (ISSN-L)
DOI: 10.1016/s0959-440x(99)00047-0
OpenAlex: W2046329541
Cited by: 317
References: 50
Citations by year: 2026: 2 · 2025: 3 · 2024: 3 · 2023: 3 · 2022: 7 · 2021: 8 · 2020: 9 · 2019: 14 · 2018: 7 · 2017: 11 · 2016: 13 · 2015: 13 · 2014: 8 · 2013: 12 · 2012: 19
FWCI: 2.02
Type: journal article
Language: en
Open access: green
figshare.com
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Current Opinion in Structural Biology (publishedVersion)
PubMed (publishedVersion)
Figshare (submittedVersion, cc-by)
Funders: Wellcome Trust
Preeclampsia Research Laboratories
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
Keywords: HSP90, molecular chaperones, ATPase activity, co-chaperones, protein folding, signaling pathways, anticancer drug targets
MeSH terms: Adenosine Triphosphate, Allosteric Regulation, Animals, Bacterial Proteins, Humans, Models, Biological, Models, Molecular, Protein Binding, Quinones, Structure-Activity Relationship, Signal Transduction, Benzoquinones, Rifabutin, HSP90 Heat-Shock Proteins, Macromolecular Substances, Lactams, Macrocyclic

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Structure and in vivo function of Hsp90

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