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Article

The effect of mutating arginine-469 on the substrate binding and refolding activities of 70-kDa heat shock cognate protein.

Archives of biochemistry and biophysics - 1 Feb 2001

Chang T C, Hsiao C D, Wu S J, Wang C

Abstract excerpt

On the basis of the X-ray structure of DnaK, we obtained an energy-minimized model for the C-terminal domain of rat 70-kDa heat shock cognate protein (hsc70). The model suggests that Arg-469 may play an important role in maintaining the substrate-bound conformation of hsc70. To verify this hypothesis, we substituted cysteine for Arg-469 and generated the hsc70(R469C) mutant. Compared to the wild-type hsc70, the...

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Identifiers

PMID: 11360998
DOI: 10.1006/abbi.2000.2176

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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