Structure and ligand recognition of the phosphotyrosine binding domain of Shc
Article Abstract:
Nuclear magnetic resonance spectroscopy of the adaptor protein Shc revealed three domains: an amino-terminal region, a collagen homology region and a carboxy-terminal SH2 homology region. Further analysis of the amino-terminal region, which is also called the phosphatyrosine binding domain, showed its ability to form antiparallel beta-strand with a beta-sheet of the protein. Analysis of the peptide in the domain revealed a structure similar to pleckstrin homology domains, suggesting a possible role in membrane localization.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1995
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NMR structure and mutagennesis of the inhibitor-of-apoptosis protein XIAP
Article Abstract:
Nuclear magnetic resonance structure research indicates that residues N-terminal to the second BIR domain, a 70-amino acid motif, might bind to to the active site of caspase-3 as the BIR domain binds to a nearby site, producing a complex of high affinity.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1999
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