title: Molecular dynamics simulations of hsp90 with an eye to inhibitor design.
abstract: Proteins carry out their functions through interactions with different partners. Dynamic conformational switching among different structural sub-states favors the adaptation to the shapes of the different partners. Such conformational changes can be determined by diverse biochemical factors, such as ligand-binding. Atomic level investigations of the mechanisms that underlie functional dynamics may provide new opportunities for the discovery of leads that target disease-related proteins. In this review, we report our views and approaches on the development of novel and accurate physical-chemistry-based models for the characterization of the salient aspects of the ligand-regulated dynamics of Hsp90, and on the exploitation of such new knowledge for the rational discovery of inhibitors of the chaperone.
authors.affiliation: Institute of Molecular Recognition Chemistry, CNR, via Mario Bianco 9, 20131 Milano, Italy. giorgio.colombo@icrm.cnr.it.
authors.forename: Elisabetta
authors.initials: E
authors.lastname: Moroni
authors.forename: Giulia
authors.initials: G
authors.lastname: Morra
authors.forename: Giorgio
authors.initials: G
authors.lastname: Colombo