1IRS

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

Summary for 1IRS

• Entry DOI: 10.2210/pdb1irs/pdb
• Descriptor: IRS-1, IL-4 RECEPTOR PHOSPHOPEPTIDE (2 entities in total)
• Functional Keywords: phosphotyrosine binding domain (ptb), complex, signal transduction, complex (signal transduction-peptide), complex (signal transduction-peptide) complex, complex (signal transduction/peptide)
• Biological source: Homo sapiens (human); More
• Cellular location: Cell membrane; Single-pass type I membrane protein. Isoform 2: Secreted: P24394
• Total number of polymer chains: 2
• Total formula weight: 13890.05

Authors

Zhou, M.-M.,Huang, B.,Olejniczak, E.T.,Meadows, R.P.,Shuker, S.B.,Miyazaki, M.,Trub, T.,Shoelson, S.E.,Feisk, S.W. (deposition date: 1996-03-22, release date: 1997-05-15, Last modification date: 2024-10-09)

Primary citation

Zhou, M.M.,Huang, B.,Olejniczak, E.T.,Meadows, R.P.,Shuker, S.B.,Miyazaki, M.,Trub, T.,Shoelson, S.E.,Fesik, S.W.
Structural basis for IL-4 receptor phosphopeptide recognition by the IRS-1 PTB domain.
Nat.Struct.Biol., 3:388-393, 1996

PubMed Abstract: 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.

PubMed: 8599766
DOI: 10.1038/nsb0496-388

Experimental method

SOLUTION NMR