The HSP90 binding mode of a radicicol-like E-oxime determined by docking, binding free energy estimations, and NMR 15N chemical shifts.

Abstract

We determine the binding mode of a macrocyclic radicicol-like oxime to yeast HSP90 by combining computer simulations and experimental measurements. We sample the macrocyclic scaffold of the unbound ligand by parallel tempering simulations and dock the most populated conformations to yeast HSP90. Docking poses are then evaluated by the use of binding free… (More)
DOI: 10.1016/j.bpc.2009.04.003

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@article{Spichty2009TheHB, title={The HSP90 binding mode of a radicicol-like E-oxime determined by docking, binding free energy estimations, and NMR 15N chemical shifts.}, author={Martin Spichty and Antoine Taly and Franz Hagn and Horst Kessler and Sofia Barluenga and Nicolas Winssinger and Martin Karplus}, journal={Biophysical chemistry}, year={2009}, volume={143 3}, pages={111-23} }