Modeling signal propagation mechanisms and ligand-based conformational dynamics of the Hsp90 molecular chaperone full-length dimer.

Modeling signal propagation mechanisms and ligand-based conformational dynamics of the Hsp90 molecular chaperone full-length dimer.

Hsp90 is a molecular chaperone essential for protein folding and activation in normal homeostasis and stress response. ATP binding and hydrolysis facilitate Hsp90 conformational changes required for client activation. Hsp90 plays an important role in disease states, particularly in cancer, where cha...

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Bibliographic Details
Main Authors: Giulia Morra, Gennady Verkhivker, Giorgio Colombo
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2009-03-01
Series:PLoS Computational Biology
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/19300478/?tool=EBI

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