Recognition of a high-affinity phosphotyrosyl peptide by the Src homology-2 domain of p56lck

[1]  I. Campbell,et al.  Structure of an SH2 domain of the p85α subunit of phosphatidylinositol-3-OH kinase , 1994, Nature.

[2]  D. Baltimore,et al.  Crystal structure of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine-phosphorylated peptides , 1993, Nature.

[3]  Arthur Weiss,et al.  ZAP-70: A 70 kd protein-tyrosine kinase that associates with the TCR ζ chain , 1992, Cell.

[4]  T. Pawson,et al.  SH2 and SH3 domains: From structure to function , 1992, Cell.

[5]  Dean R. Madden,et al.  The three-dimensional structure of HLA-B27 at 2.1 Å resolution suggests a general mechanism for tight peptide binding to MHC , 1992, Cell.

[6]  B. Margolis,et al.  Phosphatidylinositol 3′‐kinase is activated by association with IRS‐1 during insulin stimulation. , 1992, The EMBO journal.

[7]  D. Baltimore,et al.  Three-dimensional solution structure of the src homology 2 domain of c-abl , 1992, Cell.

[8]  G. Barton,et al.  Conservation analysis and structure prediction of the SH2 family of phosphotyrosine binding domains , 1992, FEBS letters.

[9]  C. Turck,et al.  Distinct phosphotyrosines on a growth factor receptor bind to specific molecules that mediate different signaling pathways , 1992, Cell.

[10]  Jonathan A. Cooper,et al.  Phosphorylation sites in the PDGF receptor with different specificities for binding GAP and PI3 kinase in vivo. , 1992, The EMBO journal.

[11]  L. Cantley,et al.  Polyoma virus middle T antigen-pp60c-src complex associates with purified phosphatidylinositol 3-kinase in vitro. , 1992, The Journal of biological chemistry.

[12]  D. Baltimore,et al.  Point mutations in the abl SH2 domain coordinately impair phosphotyrosine binding in vitro and transforming activity in vivo , 1992, Molecular and cellular biology.

[13]  A. Brunger.  Free R value: a novel statistical quantity for assessing the accuracy of crystal structures. , 1992 .

[14]  T. Yamamoto,et al.  CSK: a protein-tyrosine kinase involved in regulation of src family kinases. , 1991, The Journal of biological chemistry.

[15]  G. Kruh,et al.  Arg encodes a widely expressed 145 kDa protein-tyrosine kinase. , 1991, Oncogene.

[16]  H. Nakamura,et al.  Molecular cloning of a porcine gene syk that encodes a 72-kDa protein-tyrosine kinase showing high susceptibility to proteolysis. , 1991, The Journal of biological chemistry.

[17]  T Pawson,et al.  SH2 and SH3 domains: elements that control interactions of cytoplasmic signaling proteins. , 1991, Science.

[18]  Sefton Bm.  The lck tyrosine protein kinase. , 1991 .

[19]  J. Zou,et al.  Improved methods for building protein models in electron density maps and the location of errors in these models. , 1991, Acta crystallographica. Section A, Foundations of crystallography.

[20]  C. Turck,et al.  A phosphatidylinositol-3 kinase binds to platelet-derived growth factor receptors through a specific receptor sequence containing phosphotyrosine , 1991, Molecular and cellular biology.

[21]  L. Cantley,et al.  Oncogenes and signal transduction , 1991, Cell.

[22]  C. Chothia,et al.  The structure of protein-protein recognition sites. , 1990, The Journal of biological chemistry.

[23]  Jonathan A. Cooper,et al.  Autophosphorylation of the PDGF receptor in the kinase insert region regulates interactions with cell proteins , 1989, Cell.

[24]  S. Coughlin,et al.  Role of phosphatidylinositol kinase in PDGF receptor signal transduction. , 1989, Science.

[25]  R. Perlmutter,et al.  Structure and expression of Ick transcripts in human lymphoid cells , 1988 .

[26]  E. Krebs,et al.  A lymphocyte-specific protein-tyrosine kinase gene is rearranged and overexpressed in the murine T cell lymphoma LSTRA , 1985, Cell.

[27]  B. Lee,et al.  The interpretation of protein structures: estimation of static accessibility. , 1971, Journal of molecular biology.

[28]  G. C. Fox,et al.  An alternative method of solving the layer scaling equations of Hamilton, Rollett and Sparks , 1966 .

[29]  Axel T. Brunger,et al.  X-PLOR Version 3.1: A System for X-ray Crystallography and NMR , 1992 .

[30]  F. Studier,et al.  Use of T7 RNA polymerase to direct expression of cloned genes. , 1990, Methods in enzymology.

[31]  Axel T. Brunger,et al.  Extension of molecular replacement: a new search strategy based on Patterson correlation refinement , 1990 .

[32]  Michael G. Rossmann,et al.  The molecular replacement method : a collection of papers on the use of non-crystallographic symmetry , 1972 .