1irs

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IRS-1 PTB DOMAIN COMPLEXED WITH A IL-4 RECEPTOR PHOSPHOPEPTIDE, NMR, MINIMIZED AVERAGE STRUCTURE

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

We present the NMR structure of the PTB domain of insulin receptor, substrate-1 (IRS-1) complexed to a tyrosine-phosphorylated peptide derived, from the IL-4 receptor. Despite the lack of sequence homology and, different binding specificity, the overall fold of the protein is similar, to that of the Shc PTB domain and closely resembles that of PH domains., However, the PTB domain of IRS-1 is smaller than that of Shc (110 versus, 170 residues) and binds to phosphopeptides in a distinct manner. We, explain the phosphopeptide binding specificity based on the structure of, the complex and results of site-directed mutagenesis experiments.

Disease

Known diseases associated with this structure: AIDS, slow progression to OMIM:[147781], Atopy, susceptibility to OMIM:[147781], Coronary artery disease, susceptibility to OMIM:[147545], Diabetes mellitus, noninsulin-dependent OMIM:[147545]

About this Structure

1IRS is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structural basis for IL-4 receptor phosphopeptide recognition by the IRS-1 PTB domain., Zhou MM, Huang B, Olejniczak ET, Meadows RP, Shuker SB, Miyazaki M, Trub T, Shoelson SE, Fesik SW, Nat Struct Biol. 1996 Apr;3(4):388-93. PMID:8599766

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