Structural basis for IL-4 receptor phosphopeptide recognition by thelRS-1 PTB domain
摘要：
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 She (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.
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关键词：
Phosphotyrosine Phosphopeptides Receptors, Interleukin Receptors, Interleukin-4 Phosphoproteins Antigens, CD Magnetic Resonance Spectroscopy Mutagenesis, Site-Directed Sequence Alignment Binding Sites
DOI：
10.1038/nsb0496-388
被引量：
年份：
1996
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