ArticleChembiochem : a European journal of chemical biology2021
The Charged Linker Modulates the Conformations and Molecular Interactions of Hsp90.
Article in Chembiochem : a European journal of chemical biology, 2021. 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, 31 citations in OpenAlex.
- Backbone rigidity of disordered protein linkers from NMR experiments and MD simulations.Biophysical journal · 2026Article
- Review
- PTMs as molecular encoders: reprogramming chaperones into epichaperomes for network control in disease.Trends in biochemical sciences · 2025Review
- Heat shock proteins in osteoarthritis: molecular mechanisms, pathogenic roles, and therapeutic opportunities.Frontiers in immunology · 2025Review
- The known unknowns of the Hsp90 chaperone.eLife · 2024Review
- Extracellular heat shock protein 90 alpha (eHsp90α)'s role in cancer progression and the development of therapeutic strategies.European journal of medicinal chemistry · 2024Review
- Network pharmacology and molecular docking: combined computational approaches to explore the antihypertensive potential of Fabaceae species.Bioresources and bioprocessing · 2024Article
- Small Sized Yet Powerful: Nuclear Distribution C Proteins in Plants.Plants (Basel, Switzerland) · 2023Review
- Saccharomyces cerevisiae as a tool for deciphering Hsp90 molecular chaperone function.Essays in biochemistry · 2023Article
- Effective Molecular Dynamics from Neural Network-Based Structure Prediction Models.Journal of chemical theory and computation · 2023Article
- Visualizing the transiently populated closed-state of human HSP90 ATP binding domain.Nature communications · 2022Article
- Roles of heat-shock protein 90 and its four domains (N, LR, M and C) in calcium oxalate stone-forming processes.Cellular and molecular life sciences : CMLS · 2022Article
- Crystal structure of the middle and C-terminal domains of Hsp90α labeled with a coumarin derivative reveals a potential allosteric binding site as a drug target.Acta crystallographica. Section D, Structural biology · 2022Article
- Article
- Client binding shifts the populations of dynamic Hsp90 conformations through an allosteric network.Science advances · 2021Article
- The Potential of Hsp90 in Targeting Pathological Pathways in Cardiac Diseases.Journal of personalized medicine · 2021Review
- Inhibitors of theCells · 2021Review
- Effect of Polyphosphorylation on Behavior of Protein Disordered Regions.International journal of molecular sciences · 2021Article
- Article
- The Charged Linker Modulates the Conformations and Molecular Interactions of Hsp90.Chembiochem : a European journal of chemical biology · 2021Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The molecular chaperone Hsp90 supports the functional activity of specific substrate proteins (clients). For client processing, the Hsp90 dimer undergoes a series of ATP-driven conformational rearrangements. Flexible linkers connecting the three domains of Hsp90 are crucial to enable dynamic arrangements. The long charged linker connecting the N-terminal (NTD) and middle (MD) domains exhibits additional functions in vitro and in vivo. The structural basis for these functions remains unclear. Here, we characterize the conformation and dynamics of the linker and NTD-MD domain interactions by NMR spectroscopy. Our results reveal two regions in the linker that are dynamic and exhibit secondary structure conformation. We show that these regions mediate transient interactions with strand β8 of the NTD. As a consequence, this strand detaches and exposes a hydrophobic surface patch, which enables binding to the p53 client. We propose that the charged linker plays an important regulatory role by coupling the Hsp90 NTD-MD arrangement with the accessibility of a client binding site on the NTD.
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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.