SH2 and PTB domain interactions in tyrosine kinase signal transduction. (Q47830110)

6 February 2018

review article

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title

SH2 and PTB domain interactions in tyrosine kinase signal transduction. (English)

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6 February 2018

author name string

Shoelson SE

series ordinal

1

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6 February 2018

publication date

1 August 1997

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6 February 2018

Current Opinion in Chemical Biology

published in

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6 February 2018

volume

1

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6 February 2018

issue

2

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6 February 2018

page(s)

227-234

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6 February 2018

Protein modules and signalling networks

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SH2 domains recognize specific phosphopeptide sequences

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Specific motifs recognized by the SH2 domains of Csk, 3BP2, fps/fes, GRB-2, HCP, SHC, Syk, and Vav

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Crystal structures of peptide complexes of the amino-terminal SH2 domain of the Syp tyrosine phosphatase

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Nuclear magnetic resonance structure of an SH2 domain of phospholipase C-gamma 1 complexed with a high affinity binding peptide

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L-O-(2-malonyl)tyrosine: a new phosphotyrosyl mimetic for the preparation of Src homology 2 domain inhibitory peptides

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4'-O-[2-(2-fluoromalonyl)]-L-tyrosine: a phosphotyrosyl mimic for the preparation of signal transduction inhibitory peptides

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Insulin-stimulated oocyte maturation requires insulin receptor substrate 1 and interaction with the SH2 domains of phosphatidylinositol 3-kinase

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Spatial constraints on the recognition of phosphoproteins by the tandem SH2 domains of the phosphatase SH-PTP2

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Structural basis for specificity of Grb2-SH2 revealed by a novel ligand binding mode

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Novel phosphotyrosine mimetics in the design of peptide ligands for pp60src SH2 domain

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Discovering high-affinity ligands for proteins: SAR by NMR

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An alternative to SH2 domains for binding tyrosine-phosphorylated proteins

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Characterization of an interaction between insulin receptor substrate 1 and the insulin receptor by using the two-hybrid system

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Specificity of the PTB domain of Shc for beta turn-forming pentapeptide motifs amino-terminal to phosphotyrosine

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A phosphotyrosine interaction domain

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Role of IRS-2 in insulin and cytokine signalling

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A Novel 160-kDa Phosphotyrosine Protein in Insulin-treated Embryonic Kidney Cells Is a New Member of the Insulin Receptor Substrate Family

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Identification of the Abl- and rasGAP-associated 62 kDa protein as a docking protein, Dok

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Structure and ligand recognition of the phosphotyrosine binding domain of Shc

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Structure of the IRS-1 PTB domain bound to the juxtamembrane region of the insulin receptor

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Structure of the binding site for inositol phosphates in a PH domain

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A conserved amino-terminal Shc domain binds to phosphotyrosine motifs in activated receptors and phosphopeptides

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Activation of protein-tyrosine phosphatase SH-PTP2 by a tyrosine-based activation motif of a novel brain molecule

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A family of proteins that inhibit signalling through tyrosine kinase receptors

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Potent Activation of Phosphatidylinositol 3'-Kinase by Simple Phosphotyrosine Peptides Derived from Insulin Receptor Substrate 1 Containing Two YMXM Motifs for binding SH2 Domains

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7 January 2021

Potent stimulation of SH-PTP2 phosphatase activity by simultaneous occupancy of both SH2 domains

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Syk is activated by phosphotyrosine-containing peptides representing the tyrosine-based activation motifs of the high affinity receptor for IgE.

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Syk protein-tyrosine kinase is regulated by tyrosine-phosphorylated Ig alpha/Ig beta immunoreceptor tyrosine activation motif binding and autophosphorylation

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7 January 2021

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Identifiers

DOI

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6 February 2018

1 reference

6 February 2018