ArticleProtein science : a publication of the Protein Society2020
Hsp90 chaperones have an energetic hot-spot for binding inhibitors.
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 7 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
7 citing papers in PubMed, 11 citations in OpenAlex.
- SARS-CoV-2 Helicase (NSP13) Interacts with Mammalian Polyamine and HSP Partners in Promoting Viral Replication.Current issues in molecular biology · 2026Article
- Structural Insights into Selectively TargetingBiochemistry · 2025Article
- Selective targeting of Plasmodium falciparum Hsp90 disrupts the 26S proteasome.Cell chemical biology · 2024Article
- Exploring the antifungal potential ofFrontiers in chemistry · 2024Article
- Design, synthesis, and biological activity of dual monoamine oxidase A and heat shock protein 90 inhibitors, N-Methylpropargylamine-conjugated 4-isopropylresorcinol for glioblastoma.European journal of medicinal chemistry · 2023Article
- PlayMolecule Glimpse: Understanding Protein-Ligand Property Predictions with Interpretable Neural Networks.Journal of chemical information and modeling · 2022Article
- Hsp90 chaperones have an energetic hot-spot for binding inhibitors.Protein science : a publication of the Protein Society · 2020Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Although Hsp90-family chaperones have been extensively targeted with ATP-competitive inhibitors, it is unknown whether high affinity is achieved from a few highly stabilizing contacts or from many weaker contacts within the ATP-binding pocket. A large-scale analysis of Hsp90α:inhibitor structures shows that inhibitor hydrogen-bonding to a conserved aspartate (D93 in Hsp90α) stands out as most universal among Hsp90 inhibitors. Here we show that the D93 region makes a dominant energetic contribution to inhibitor binding for both cytosolic and organelle-specific Hsp90 paralogs. For inhibitors in the resorcinol family, the D93:inhibitor hydrogen-bond is pH-dependent because the associated inhibitor hydroxyl group is titratable, rationalizing a linked-protonation event previously observed by the Matulis group. The inhibitor hydroxyl group pK
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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.