Pathways of allosteric regulation in Hsp70 chaperones.
Heidelberg, Germany. In Nat Commun, 2014
Central to the protein folding activity of Hsp70 chaperones is their ability to interact with protein substrates in an ATP-controlled manner, which relies on allosteric regulation between their nucleotide-binding (NBD) and substrate-binding domains (SBD).
Insights into the molecular mechanism of allostery in Hsp70s.
Heidelberg, Germany. In Front Mol Biosci, 2014
Key to their versatility is the recognition of a short degenerate sequence motif, present in practically all polypeptides, and a bidirectional allosteric intramolecular regulation mechanism linking their N-terminal nucleotide binding domain (NBD) and their C-terminal polypeptide substrate binding domain (SBD).
Hsp70 chaperone dynamics and molecular mechanism.
Heidelberg, Germany. In Trends Biochem Sci, 2013
The chaperone functions of heat shock protein (Hsp)70 involve an allosteric control mechanism between the nucleotide-binding domain (NBD) and polypeptide substrate-binding domain (SBD): ATP binding and hydrolysis regulates the affinity for polypeptides, and polypeptide binding accelerates ATP hydrolysis.
Inhibitors of Protein Folding: DnaK
Bethesda, United States. In Unknown Journal, 2009
Specifically, these probes would alter DnaK through interactions with its substrate-binding domain (SBD).