Structure of an SH2 domain of the p85 alpha subunit of phosphatidylinositol-3-OH kinase (Q27642078)

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A L Breeze

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A K Downing

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G Panayotou

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I Gout

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M D Waterfield

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I D Campbell

Signal transduction by receptors with tyrosine kinase activity

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language of work or name

English

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publication date

20 August 1992

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published in

Nature

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volume

358

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issue

6388

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page(s)

684-7

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cites work

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Oncogenes and signal transduction

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SH2 and SH3 domains: elements that control interactions of cytoplasmic signaling proteins

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Distinct phosphotyrosines on a growth factor receptor bind to specific molecules that mediate different signaling pathways

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Point mutations in the abl SH2 domain coordinately impair phosphotyrosine binding in vitro and transforming activity in vivo

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Characterization of two 85 kd proteins that associate with receptor tyrosine kinases, middle-T/pp60c-src complexes, and PI3-kinase

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Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase

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Conservation analysis and structure prediction of the SH2 family of phosphotyrosine binding domains

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Overcoming the overlap problem in the assignment of 1H NMR spectra of larger proteins by use of three-dimensional heteronuclear 1H-15N Hartmann-Hahn-multiple quantum coherence and nuclear Overhauser-multiple quantum coherence spectroscopy: applicati

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Complete resonance assignment for the polypeptide backbone of interleukin 1.beta. using three-dimensional heteronuclear NMR spectroscopy

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Protein secondary structure determination by NMR. Application with recombinant human cyclophilin.

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The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy

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Solution conformations of human growth hormone releasing factor: comparison of the restrained molecular dynamics and distance geometry methods for a system without long-range distance data

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Determination of three-dimensional structures of proteins by simulated annealing with interproton distance restraints. Application to crambin, potato carboxypeptidase inhibitor and barley serine proteinase inhibitor 2.

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Solution structure of the fibrin binding finger domain of tissue-type plasminogen activator determined by 1H nuclear magnetic resonance

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Determination of three-dimensional structures of proteins from interproton distance data by hybrid distance geometry-dynamical simulated annealing calculations

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CHARMM: A program for macromolecular energy, minimization, and dynamics calculations

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SH2 domains of the p85 alpha subunit of phosphatidylinositol 3-kinase regulate binding to growth factor receptors

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Pseudo-structures for the 20 common amino acids for use in studies of protein conformations by measurements of intramolecular proton-proton distance constraints with nuclear magnetic resonance

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Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA

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MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

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