Structural basis for IL-4 receptor phosphopeptide recognition by the IRS-1 PTB domain

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...

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Veröffentlicht in:	Nature structural biology 1996-04, Vol.3 (4), p.388
Hauptverfasser:	Zhou, M M, Huang, B, Olejniczak, E T, Meadows, R P, Shuker, S B, Miyazaki, M, Trüb, T, Shoelson, S E, Fesik, S W
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Antigens, CD - chemistry Antigens, CD - metabolism Binding Sites Insulin Receptor Substrate Proteins Magnetic Resonance Spectroscopy Models, Molecular Molecular Sequence Data Mutagenesis, Site-Directed Phosphopeptides - chemistry Phosphopeptides - metabolism Phosphoproteins - chemistry Phosphoproteins - genetics Phosphoproteins - metabolism Phosphotyrosine - metabolism Protein Conformation Protein Structure, Tertiary Receptors, Interleukin - chemistry Receptors, Interleukin - metabolism Receptors, Interleukin-4 Sequence Alignment
Online-Zugang:	Volltext
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