ArticleProtein science : a publication of the Protein Society2020
Molecular basis of the interaction of Hsp90 with its co-chaperone Hop.
Article in Protein science : a publication of the Protein Society, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 25 citations in OpenAlex.
- Rearrangement of the Cell Chaperone Machinery in Human Fibrosarcoma HT1080 Cells With the Knocked-Out HSP90AA1 Gene Encoding Hsp90α.Biology of the cell · 2026Article
- Seasonal diet shifts alter the gut microbiome and resistome of captive geriatric giant pandas (Ailuropoda melanoleuca).BMC microbiology · 2026Article
- Review
- Hsp90Pharmaceuticals (Basel, Switzerland) · 2025Review
- Chaperone-dependent and chaperone-independent functions of carboxylate clamp tetratricopeptide repeat (CC-TPR) proteins.Trends in biochemical sciences · 2025Review
- Insights into the Allosteric Regulation of Human Hsp90 Revealed by NMR Spectroscopy.Biomolecules · 2024Review
- Hsp90, a team player in protein quality control and the stress response in bacteria.Microbiology and molecular biology reviews : MMBR · 2024Review
- The multi-faceted roles of R2TP complex span across regulation of gene expression, translation, and protein functional assembly.Biophysical reviews · 2023Review
- Hsp multichaperone complex buffers pathologically modified Tau.Nature communications · 2022Article
- Assembly mechanism of early Hsp90-Cdc37-kinase complexes.Science advances · 2022Article
- Heat Shock Proteins in Benign Prostatic Hyperplasia and Prostate Cancer.International journal of molecular sciences · 2022Review
- Identification of quantitative trait loci for survival in the mutant dynactin p150Glued mouse model of motor neuron disease.PloS one · 2022Article
- The STI1-domain is a flexible alpha-helical fold with a hydrophobic groove.Protein science : a publication of the Protein Society · 2021Article
- Structural Communication between theInternational journal of molecular sciences · 2021Article
- Mechanistic Insights into the Role of Molecular Chaperones in Protein Misfolding Diseases: From Molecular Recognition to Amyloid Disassembly.International journal of molecular sciences · 2020Review
- Molecular basis of the interaction of Hsp90 with its co-chaperone Hop.Protein science : a publication of the Protein Society · 2020Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The heat shock protein (Hsp) Hsp90 is one of the most abundant proteins in the cell. It controls the functional turnover of proteins being involved in protein folding, refolding, transport as well as protein degradation. Co-chaperones influence Hsp90's activity in different ways, among which the Hsp organizing protein (Hop) was found to inhibit its ATP hydrolysis upon binding. Despite the availability of a number of studies investigating the Hsp90:Hop complex, several aspects of the Hsp90:Hop interaction have remained unresolved. Here, we employed a combinatory approach comprising native polyacrylamide gel electrophoresis, isothermal titration calorimetry, multiangle light scattering, isothermal titration calorimetry, small-angle X-ray scattering, dynamic light scattering, and nuclear magnetic resonance, spectroscopy to obtain a comprehensive picture about the human Hsp90β:Hop association in solution. Our data show that only one Hop molecule binds the Hsp90β dimer, Hop can interact with the open and closed state of Hsp90β, and Hop's TPR2A-2B domains determine the affinity for Hsp90's C-terminal and middle domain, whereby the interaction with the C-terminal domain of Hsp90β is sufficient to induce an allosteric conformational change between the two Hsp90β monomers in the Hsp90
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Registered trials
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.