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, TrĂ¼b T, Shoelson SE, Fesik SW
Nat Struct Biol. 1996 3 (4): 388-93

PMID: 8599766 · DOI:10.1038/nsb0496-388

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.

MeSH Terms (16)

Amino Acid Sequence Antigens, CD Binding Sites Insulin Receptor Substrate Proteins Magnetic Resonance Spectroscopy Models, Molecular Molecular Sequence Data Mutagenesis, Site-Directed Phosphopeptides Phosphoproteins Phosphotyrosine Protein Conformation Protein Structure, Tertiary Receptors, Interleukin Receptors, Interleukin-4 Sequence Alignment

Connections (1)

This publication is referenced by other Labnodes entities: