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TitleStructural basis for the recognition of the two NKG2A immunoreceptor tyrosine-based inhibitory motifs (ITIMs) by the C-terminal SH2 domain of protein tyrosine phosphatase SHP-1
Journal, issue, pagesTo be Published
Publish dateNov 30, 2007 (structure data deposition date)
AuthorsKoshiba, S. / Kasai, T. / Sato, M. / Tomizawa, T. / Motoda, Y. / Tochio, N. / Kobayashi, N. / Harada, T. / Inoue, M. / Tanaka, A. ...Koshiba, S. / Kasai, T. / Sato, M. / Tomizawa, T. / Motoda, Y. / Tochio, N. / Kobayashi, N. / Harada, T. / Inoue, M. / Tanaka, A. / Kigawa, T. / Yokoyama, S.
External linksSearch PubMed
MethodsNMR (solution)
Structure data

PDB-2rmx:
Solution structure of the SHP-1 C-terminal SH2 domain complexed with a tyrosine-phosphorylated peptide from NKG2A
Method: SOLUTION NMR

Source
  • homo sapiens (human)
KeywordsSIGNALING PROTEIN / SH2 domain / protein-peptide complex / phosphorylated peptide recognition / phosphotyrosine binding domain / signal transduction / Alternative splicing / Cytoplasm / Hydrolase / Nucleus / Phosphoprotein / Protein phosphatase / Glycoprotein / Lectin / Membrane / Receptor / Signal-anchor / Transmembrane / Structural Genomics / NPPSFA / National Project on Protein Structural and Functional Analyses / RIKEN Structural Genomics/Proteomics Initiative / RSGI

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