Curr Opin Struct Biol 10(1):46–51Įcheverria PC, Picard D (2010) Molecular chaperones, essential partners of steroid hormone receptors for activity and mobility. Pearl LH, Prodromou C (2000) Structure and in vivo function of Hsp90. Keywordsīurrows F, Zhang H et al (2004) Hsp90 activation and cell cycle regulation. This review discusses all these aspects of Hsp90 structure and function. The system is also regulated by post-translational modifications including phosphorylation and acetylation. It also uses a host of cochaperones which not only regulate the ATPase activity and conformational dynamics but which also mediate interactions with Hsp90 client proteins. As with many of the other classes of molecular chaperone, Hsp90 has a critical ATPase activity, and ATP binding and hydrolysis known to modulate the conformational dynamics of the protein. The focus of this review is the structural and mechanistic studies which have been performed in order to understand how this important chaperone acts on a wide variety of different proteins (its client proteins) and cellular processes. In the last ten years, it has become a major therapeutic target for cancer, and there has also been increasing interest in it as a therapeutic target in neurodegenerative disorders, and in the development of anti-virals and anti-protozoan infections. It is important for the cell’s response to stress and is a key player in maintaining cellular homeostasis. Hsp90 is a highly abundant and ubiquitous molecular chaperone which plays an essential role in many cellular processes including cell cycle control, cell survival, hormone and other signalling pathways.
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