Dynamics of conserved waters in human Hsp90: implications for drug design.
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.
Yan
Aixia
A
Department of Chemistry, Central Chemistry Laboratory, University of Oxford, South Parks Road, Oxford, UK.
Grant
Guy H
GH
Richards
W Graham
WG
D000225:Adenine / Q000031:analogs & derivatives* / Q000737:chemistry; D000840:Anisoles / Q000737:chemistry*; D003198:Computer Simulation; D015195:Drug Design; D018841:HSP90 Heat-Shock Proteins / Q000737:chemistry*; D006801:Humans; D008958:Models, Molecular; D010100:Oxygen / Q000737:chemistry; D014867:Water / Q000737:chemistry*
C494601:9-(n-butyl)-8-((3,4,5-trimethoxyphenyl)methyl)adenine; D000840:Anisoles; D018841:HSP90 Heat-Shock Proteins; D014867:Water; D000225:Adenine; D010100:Oxygen