PMID:8061603

Citation	Topping, TB and Randall, LL (1994) Determination of the binding frame within a physiological ligand for the chaperone SecB. Protein Sci. 3:730-6
Abstract	The hallmark of the class of proteins called chaperones is the amazing ability to bind tightly to a wide array of polypeptide ligands that have no consensus in sequence; chaperones recognize non-native structure. As a step in the elucidation of the molecular mechanism of such remarkable binding, we have characterized complexes between the bacterial chaperone SecB and a series of ligands related to maltose-binding protein. SecB interacts at multiple sites on its polypeptide ligand. The entire binding region covers approximately half of the primary sequence of maltose-binding protein and comprises contiguous sites positioned around the center of the sequence.
Links	PubMed PMC2142715 Online version:10.1002/pro.5560030502
Keywords	ATP-Binding Cassette Transporters; Amino Acid Sequence; Bacterial Proteins/chemistry; Bacterial Proteins/metabolism; Binding Sites; Carrier Proteins/chemistry; Carrier Proteins/metabolism; Escherichia coli/metabolism; Escherichia coli Proteins; Ligands; Maltose/metabolism; Maltose-Binding Proteins; Molecular Structure; Molecular Weight; Monosaccharide Transport Proteins; Protein Binding; Protein Precursors/chemistry; Protein Precursors/metabolism
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