Binding of a Small Molecule at a Protein–Protein Interface Regulates the Chaperone Activity of Hsp70–Hsp40

Heat shock protein 70 (Hsp70) is a highly conserved molecular chaperone that plays multiple roles in protein homeostasis. In these various tasks, the activity of Hsp70 is shaped by interactions with co-chaperones, such as Hsp40. The Hsp40 family of co-chaperones binds to Hsp70 through a conserved J-...

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Veröffentlicht in:ACS chemical biology 2010-06, Vol.5 (6), p.611-622
Hauptverfasser: Wisén, Susanne, Bertelsen, Eric B, Thompson, Andrea D, Patury, Srikanth, Ung, Peter, Chang, Lyra, Evans, Christopher G, Walter, Gladis M, Wipf, Peter, Carlson, Heather A, Brodsky, Jeffrey L, Zuiderweg, Erik R. P, Gestwicki, Jason E
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Sprache:eng
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