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

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. Copyright © 1994 The Protein Society