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Article

The four hydrophobic residues on the Hsp70 inter-domain linker have two distinct roles.

Journal of molecular biology - 2 Sept 2011

Kumar Divya Prasanna, Vorvis Christina, Sarbeng Evans Boateng, Cabra Ledesma Vanessa C, Willis John Eric, Liu Qinglian

Abstract excerpt

The ubiquitous molecular chaperone 70-kDa heat shock proteins (Hsp70) play key roles in maintaining protein homeostasis. Hsp70s contain two functional domains: a nucleotide binding domain and a substrate binding domain. The two domains are connected by a highly conserved inter-domain linker, and allosteric coupling between the two domains is critical for chaperone function. The auxiliary chaperone 40-kDa heat...

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Identifiers

PMID: 21762702
DOI: 10.1016/j.jmb.2011.07.001
PMCID: PMC5737734

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