Corresponding functional dynamics across the Hsp90 Chaperone family: insights from a multiscale analysis of MD simulations.

ABSTRACT: Understanding how local protein modifications, such as binding small-molecule ligands, can trigger and regulate large-scale motions of large protein domains is a major open issue in molecular biology. We address various aspects of this problem by analyzing and comparing atomistic simulations of Hsp90 family representatives for which crystal structures of the full length protein are available: mammalian Grp94, yeast Hsp90 and E.coli HtpG. These chaperones are studied in complex with the natural ligands ATP, ADP and in the Apo state. Common key aspects of their functional dynamics are elucidated with a novel multi-scale comparison of their internal dynamics. Starting from the atomic resolution investigation of internal fluctuations and geometric strain patterns, a novel analysis of domain dy

SUBMITTER: Morra G 

PROVIDER: S-EPMC3310708 | biostudies-literature | 2012

REPOSITORIES: biostudies-literature