Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/94261
Title: Solution structure of the Shc SH2 domain complexed with a tyrosine-phosphorylated peptide from the T-cell receptor
Authors: Meadows, Robert P.
Logan, Timothy M.
Wade, Warren S.
Ravichandran, Kodimangalam S.
Burakoffe, Steven J.
Fesik, Stephen W.
Zhou, Ming-Ming
Yoon, Ho Sup
Keywords: DRNTU::Science::Biological sciences
Issue Date: 1995
Source: Zhou, M. M., Meadows, R. P., Logan, T. M., Yoon, H. S., Wade, W. S., Ravichandran, K. S., et al. (1995). Solution structure of the Shc SH2 domain complexed with a tyrosine-phosphorylated peptide from the T-cell receptor. Proceedings of the National Academy of Sciences, 92(17), 7784-7788.
Abstract: Shc 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.
URI: https://hdl.handle.net/10356/94261
http://hdl.handle.net/10220/7506
DOI: 10.1073/pnas.92.17.7784
Rights: © 1995 National Academy of Sciences. This is the author created version of a work that has been peer reviewed and accepted for publication by Proceedings of the National Academy of Sciences , National Academy of Sciences.  It incorporates referee’s comments but changes resulting from the publishing process, such as copyediting, structural formatting, may not be reflected in this document.  The published version is available at: http://dx.doi.org/10.1073/pnas.92.17.7784
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:SBS Conference Papers

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