Ontology highlight
ABSTRACT:
SUBMITTER: Stevens SY
PROVIDER: S-EPMC2366956 | biostudies-other | 2003 Nov
REPOSITORIES: biostudies-other
Stevens Shawn Y SY Cai Sheng S Pellecchia Maurizio M Zuiderweg Erik R P ER
Protein science : a publication of the Protein Society 20031101 11
The Hsp70 family of molecular chaperones participates in a number of cellular processes, including binding to nascent polypeptide chains and assistance in protein (re)folding and degradation. We present the solution structure of the substrate binding domain (residues 393-507) of the Escherichia coli Hsp70, DnaK, that is bound to the peptide NRLLLTG and compare it to the crystal structure of DnaK(389-607) bound to the same peptide. The construct discussed here does not contain the alpha-helical d ...[more]