Solution structure of the Shc SH2 domain complexed with a tyrosine-phosphorylated peptide from the T-cell receptor.

Zhou MM, Meadows RP, Logan TM, Yoon HS, Wade WS, Ravichandran KS, Burakoff SJ, Fesik SW
Proc Natl Acad Sci U S A. 1995 92 (17): 7784-8

PMID: 7544002 · PMCID: PMC41230 · DOI:10.1073/pnas.92.17.7784

She is a widely expressed adapter protein that plays an important role in signaling via a variety of cell surface receptors and has been implicated in coupling the stimulation of growth factor, cytokine, and antigen receptors to the Ras signaling pathway. She interacts with several tyrosine-phosphorylated receptors through its C-terminal SH2 domain, and one of the mechanisms of T-cell receptor-mediated Ras activation involves the interaction of the Shc SH2 domain with the tyrosine-phosphorylated zeta chain of the T-cell receptor. Here we describe a high-resolution NMR structure of the Shc SH2 domain complexed to a phosphopeptide (GHDGLpYQGLSTATK) corresponding to a portion of the zeta chain of the T-cell receptor. Although the overall architecture of the protein is similar to other SH2 domains, distinct structural differences were observed in the smaller beta-sheet, BG loop, (pY + 3) phosphopeptide-binding site, and relative position of the bound phosphopeptide.

MeSH Terms (23)

Adaptor Proteins, Signal Transducing Adaptor Proteins, Vesicular Transport Amino Acid Sequence Animals Binding Sites Cloning, Molecular Conserved Sequence Magnetic Resonance Spectroscopy Models, Molecular Molecular Sequence Data Peptide Fragments Phosphopeptides Phosphorylation Phosphotyrosine Protein Conformation Proteins Protein Structure, Secondary Receptors, Antigen, T-Cell Recombinant Proteins Sequence Homology, Amino Acid Shc Signaling Adaptor Proteins Solutions Tyrosine

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