Interaction of Hsp70 chaperones with substrates
- 1 May 1997
- journal article
- review article
- Published by Springer Nature in Nature Structural & Molecular Biology
- Vol. 4 (5), 342-349
- https://doi.org/10.1038/nsb0597-342
Abstract
Determination of the structure of the substrate binding domain of the Escherichia coli Hsp70 chaperone, DnaK, and the biochemical characterisation of the motif it recognizes within substrates provide insights into the principles governing Hsp70 interaction with polypeptide chains. DnaK recognizes extended peptide strands composed of up to five consecutive hydrophobic residues within and positively charged residues outside the substrate binding cavity.Keywords
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