Mutations in the Hsp90 N Domain Identify a Site that Controls Dimer Opening and Expand Human Hsp90α Function in Yeast.

Abstract excerpt

Hsp90 is a highly conserved molecular chaperone important for the activity of many client proteins. Hsp90 has an N-terminal ATPase domain (N), a middle domain (M) that interacts with clients and a C-terminal dimerization domain (C). "Closing" of dimers around clients is regulated by ATP binding, co-chaperones, and post-translational modifications. ATP hydrolysis coincides with release of mature client and...

Topics

• Adenosine Triphosphate
• Binding Sites
• Cloning, Molecular
• Peptidyl-Prolyl Isomerase F
• Gene Expression Regulation
• HSP90 Heat-Shock Proteins
• Humans
• Models, Molecular
• Molecular Chaperones
• Mutation
• Protein Binding