Solution structure of the Shc SH2 domain complexed with a tyrosine-phosphorylated peptide from the T-cell receptor (Q27729434)

1

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R P Meadows

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T M Logan

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H S Yoon

4

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W S Wade

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K S Ravichandran

6

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S W Fesik

Proceedings of the National Academy of Sciences of the United States of America

8

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language of work or name

English

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publication date

15 August 1995

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published in

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volume

92

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issue

17

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page(s)

7784-8

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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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A novel transforming protein (SHC) with an SH2 domain is implicated in mitogenic signal transduction

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The adapter protein Shc interacts with the interleukin-2 (IL-2) receptor upon IL-2 stimulation

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Direct interaction between Shc and the platelet-derived growth factor beta-receptor

20 March 2017

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A novel approach for sequential assignment of 1H, 13C, and 15N spectra of proteins: heteronuclear triple-resonance three-dimensional NMR spectroscopy. Application to calmodulin

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An efficient 3D NMR technique for correlating the proton and 15N backbone amide resonances with the alpha-carbon of the preceding residue in uniformly 15N/13C enriched proteins

20 March 2017

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B cell antigen receptor stimulation induces formation of a Shc-Grb2 complex containing multiple tyrosine-phosphorylated proteins

20 March 2017

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Involvement of Src-homology/collagen (SHC) proteins in signaling through the insulin receptor and the insulin-like-growth-factor-I-receptor

20 March 2017

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

20 March 2017

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Stereospecific nuclear magnetic resonance assignments of the methyl groups of valine and leucine in the DNA-binding domain of the 434 repressor by biosynthetically directed fractional 13C labeling

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Tautomeric states of the active-site histidines of phosphorylated and unphosphorylated IIIGlc, a signal-transducing protein from Escherichia coli, using two-dimensional heteronuclear NMR techniques

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Neuronal differentiation signals are controlled by nerve growth factor receptor/Trk binding sites for SHC and PLC gamma.

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Trk receptors use redundant signal transduction pathways involving SHC and PLC-gamma 1 to mediate NGF responses

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Structures of larger proteins, protein-ligand and protein-DNA complexes by multi-dimensional heteronuclear NMR.

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A region in Shc distinct from the SH2 domain can bind tyrosine-phosphorylated growth factor receptors.

29 September 2017

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An alternative to SH2 domains for binding tyrosine-phosphorylated proteins

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Determination of three-dimensional structures of proteins from interproton distance data by dynamical simulated annealing from a random array of atoms. Circumventing problems associated with folding

29 September 2017

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Interaction of Shc with the zeta chain of the T cell receptor upon T cell activation

29 September 2017

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Interleukin-2-induced tyrosine phosphorylation of p52shc in T lymphocytes.

2 June 2018

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Identification of residues in GTPase-activating protein Src homology 2 domains that control binding to tyrosine phosphorylated growth factor receptors and p62.

2 June 2018

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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

2 June 2018

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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

19 June 2018

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PubMed

https://pubmed.ncbi.nlm.nih.gov/7544002

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Side chain and backbone assignments in isotopically labeled proteins from two heteronuclear triple resonance experiments

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/7544002

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Epidermal growth factor stimulates the tyrosine phosphorylation of SHC in the mouse

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/7544002