Specificity in substrate binding by protein folding catalysts: Tyrosine and tryptophan residues are the recognition motifs for the binding of peptides to the pancreas-specific protein disulfide isomerase PDIp

Ruddock, L.W. and Freedman, R.B. and Klappa, P. (2000) Specificity in substrate binding by protein folding catalysts: Tyrosine and tryptophan residues are the recognition motifs for the binding of peptides to the pancreas-specific protein disulfide isomerase PDIp. Protein Science, 9 (4). pp. 758-764. ISSN 0961-8368. (The full text of this publication is not available from this repository)

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Abstract

Using a cross-linking approach, we recently demonstrated that radiolabeled peptides or misfolded proteins specifically interact in vitro with two luminal proteins in crude extracts from pancreas microsomes. The proteins were the folding catalysts protein disulfide isomerase (PDI) and PDIp, a glycosylated, PDI-related protein, expressed exclusively in the pancreas. In this study, we explore the specificity of these proteins in binding peptides and related ligands and show that tyrosine and tryptophan residues in peptides are the recognition motifs for their binding by PDIp. This peptide-binding specificity may reflect the selectivity of PDIp in binding regions of unfolded polypeptide during catalysis of protein folding.

Item Type: Article
Uncontrolled keywords: cross-linking; peptide binding; protein disulfide isomerase; tryptophan; tyrosine
Subjects: Q Science > QP Physiology (Living systems) > QP517 Biochemistry
Q Science > QP Physiology (Living systems) > QP506 Molecular biology
Divisions: Faculties > Science Technology and Medical Studies > School of Biosciences
Depositing User: A. Xie
Date Deposited: 27 Jun 2009 21:35
Last Modified: 27 Jun 2009 21:35
Resource URI: http://kar.kent.ac.uk/id/eprint/16590 (The current URI for this page, for reference purposes)
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