Premium
Determination of the binding frame within a physiological ligand for the chaperone SecB
Author(s) -
Topping Traci B.,
Randall Linda L.
Publication year - 1994
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5560030502
Subject(s) - chaperone (clinical) , maltose binding protein , biochemistry , binding site , chemistry , co chaperone , plasma protein binding , ligand (biochemistry) , sequence (biology) , biophysics , biology , fusion protein , hsp90 , receptor , recombinant dna , heat shock protein , medicine , pathology , gene
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.