Dynamics of conserved waters in human Hsp90: implications for drug design

Abstract

The flexibility of a promising protein target, human heat shock protein 90 (Hsp90), is investigated by molecular dynamics simulations. These simulations focus on: (i) the interactions between the protein and conserved water molecules; and (ii) the interactions of the ligand PU3, the conserved water molecules and the protein. This is followed by a virtual screening docking study of the PU3 family of compounds and Hsp90 incorporating several conserved water molecules

Similar works

Full text

PubMed CentralProvided a free PDF (195.62 KB)

2586097oai:pubmedcentral.nih.gov:2586097
Last time updated on July 8, 2012View original full text link

This paper was published in PubMed Central.

Having an issue?

Is data on this page outdated, violates copyrights or anything else? Report the problem now and we will take corresponding actions after reviewing your request.