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Updated: Aug 4, 2026

Studies of Chaperone-Cochaperone Interactions using Homogenous Bead-Based Assay
Published on: July 21, 2021
Structure-based discovery of a new class of Hsp90 inhibitors
Xavier Barril1, Paul Brough, Martin Drysdale
1Vernalis (R&D) Ltd, Granta Park, Abington, Cambridge CB1 6GB, UK. x.barril@vernalis.com
Abstract:
Docking-based virtual screening identified 1-(2-phenol)-2-naphthol compounds as a new class of Hsp90 inhibitors of low to sub-micromolar potency. Here we report the binding affinities and cellular activities of several members of this class. A high resolution crystal structure of the most potent compound reveals its binding mode in the ATP binding site of Hsp90, providing a rationale for the observed activity of the series and suggesting strategies for developing compounds with improved properties.
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