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Crystal structure of the tyrosine phosphatase SHP-2
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scholarly article
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title
Crystal structure of the tyrosine phosphatase SHP-2
(English)
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main subject
crystal structure
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author name string
P Hof
series ordinal
1
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S Pluskey
series ordinal
2
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S Dhe-Paganon
series ordinal
3
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M J Eck
series ordinal
4
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S E Shoelson
series ordinal
5
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language of work or name
English
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publication date
20 February 1998
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published in
Cell
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volume
92
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page(s)
441-50
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issue
4
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cites work
Insulin signaling in mice expressing reduced levels of Syp.
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Thermodynamic and structural compensation in "size-switch" core repacking variants of bacteriophage T4 lysozyme
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Crystal structure of human protein tyrosine phosphatase 1B
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Multiple requirements for SHPTP2 in epidermal growth factor-mediated cell cycle progression
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Structural basis for inhibition of receptor protein-tyrosine phosphatase-alpha by dimerization
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Modular binding domains in signal transduction proteins
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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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Response of a protein structure to cavity-creating mutations and its relation to the hydrophobic effect
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SH2-containing phosphotyrosine phosphatase as a target of protein-tyrosine kinases
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A novel membrane glycoprotein, SHPS-1, that binds the SH2-domain-containing protein tyrosine phosphatase SHP-2 in response to mitogens and cell adhesion
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The crystal structure of domain 1 of receptor protein-tyrosine phosphatase mu
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Structure of the hydrophobic core in the transition state for folding of chymotrypsin inhibitor 2: a critical test of the protein engineering method of analysis
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Effect of cavity-creating mutations in the hydrophobic core of chymotrypsin inhibitor 2
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Characterization of phosphotyrosine binding motifs in the cytoplasmic domain of platelet/endothelial cell adhesion molecule-1 (PECAM-1) that are required for the cellular association and activation of the protein-tyrosine phosphatase, SHP-2
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Structural basis for phosphotyrosine peptide recognition by protein tyrosine phosphatase 1B
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A family of proteins that inhibit signalling through tyrosine kinase receptors
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MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures
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Modular peptide recognition domains in eukaryotic signaling
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Crystal structures of peptide complexes of the amino-terminal SH2 domain of the Syp tyrosine phosphatase
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Protein tyrosine phosphatases in signal transduction.
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Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons
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Structural determinants of SHP-2 function and specificity in Xenopus mesoderm induction
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Tandem SH2 domains confer high specificity in tyrosine kinase signaling
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Protein modules and signalling networks
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Intramolecular regulation of protein tyrosine phosphatase SH-PTP1: a new function for Src homology 2 domains
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Differential functions of the two Src homology 2 domains in protein tyrosine phosphatase SH-PTP1
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corkscrew encodes a putative protein tyrosine phosphatase that functions to transduce the terminal signal from the receptor tyrosine kinase torso
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Potent stimulation of SH-PTP2 phosphatase activity by simultaneous occupancy of both SH2 domains
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Identification of structural motifs from protein coordinate data: secondary structure and first-level supersecondary structure
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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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Abnormal mesoderm patterning in mouse embryos mutant for the SH2 tyrosine phosphatase Shp-2.
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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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Identifiers
DOI
10.1016/S0092-8674(00)80938-1
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PubMed ID
9491886
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