Protein Science, Vol 3, Issue 5 730-736, Copyright © 1994 by Cold Spring Harbor Laboratory Press

ARTICLE

Determination of the binding frame within a physiological ligand for the chaperone SecB

T. B. TOPPING and L. L. RANDALL
Department of Biochemistry and Biophysics, Washington State University, Pullman, Washington 99164-4660

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.
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