1tce
From Proteopedia
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SOLUTION NMR STRUCTURE OF THE SHC SH2 DOMAIN COMPLEXED WITH A TYROSINE-PHOSPHORYLATED PEPTIDE FROM THE T-CELL RECEPTOR, MINIMIZED AVERAGE STRUCTURE
Contents |
Overview
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.
Disease
Known disease associated with this structure: Immunodeficiency due to defect in CD3-zeta OMIM:[186780]
About this Structure
1TCE is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.
Reference
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 Aug 15;92(17):7784-8. PMID:7544002
Page seeded by OCA on Mon Nov 12 19:23:22 2007
