Science. 1992 Jul 10;257(5067):241-5.

Peptide binding by chaperone SecB: implications for recognition of nonnative structure.

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Department of Biochemistry and Biophysics, Washington State University, Pullman 99164-4660.

Abstract

The molecular basis for recognition of nonnative proteins by the molecular chaperone SecB was investigated with an in vitro assay based on the protection of SecB from proteolysis when a ligand is bound. The SecB tetramer has multiple binding sites for positively charged peptides. When the peptide binding sites are occupied, the complex undergoes a conformational change to expose hydrophobic sites that bind the fluorescent probe 1-anilinonaphthalene-8-sulfonate. A model is proposed for interaction of nonnative polypeptides with both hydrophilic and hydrophobic sites on SecB.

PMID:: 1631545; [PubMed - indexed for MEDLINE]

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GM29798/GM/NIGMS NIH HHS/United States

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