1TCE

SOLUTION NMR STRUCTURE OF THE SHC SH2 DOMAIN COMPLEXED WITH A TYROSINE-PHOSPHORYLATED PEPTIDE FROM THE T-CELL RECEPTOR, MINIMIZED AVERAGE STRUCTURE

Summary for 1TCE

• Entry DOI: 10.2210/pdb1tce/pdb
• Descriptor: SHC, PHOSPHOPEPTIDE OF THE ZETA CHAIN OF T CELL RECEPTOR (2 entities in total)
• Functional Keywords: sh2 domain, complex (signal transduction-peptide), complex (signal transduction-peptide) complex, complex (signal transduction/peptide)
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm. Isoform p46Shc: Mitochondrion matrix. Isoform p66Shc: Mitochondrion (By similarity): P29353; Membrane; Single-pass type I membrane protein: P20963
• Total number of polymer chains: 2
• Total formula weight: 13653.22

Authors

Zhou, M.-M.,Meadows, R.P.,Logan, T.M.,Yoon, H.S.,Wade, W.R.,Ravichandran, K.S.,Burakoff, S.J.,Feisk, S.W. (deposition date: 1996-03-27, release date: 1997-05-15, Last modification date: 2024-10-30)

Primary citation

Zhou, M.M.,Meadows, R.P.,Logan, T.M.,Yoon, H.S.,Wade, W.S.,Ravichandran, K.S.,Burakoff, S.J.,Fesik, S.W.
Solution structure of the Shc SH2 domain complexed with a tyrosine-phosphorylated peptide from the T-cell receptor.
Proc.Natl.Acad.Sci.USA, 92:7784-7788, 1995

PubMed Abstract: 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.

PubMed: 7544002
DOI: 10.1073/pnas.92.17.7784

Experimental method

SOLUTION NMR