Abstract
The nuclear magnetic resonance structure of the phosphotyrosine binding (PTB) domain of Shc complexed to a phosphopeptide reveals an alternative means of recognizing tyrosine-phosphorylated proteins. Unlike in SH2 domains, the phosphopeptide forms an antiparallel beta-strand with a beta-sheet of the protein, interacts with a hydrophobic pocket through the (pY-5) residue, and adopts a beta-turn. The PTB domain is structurally similar to pleckstrin homology domains (a beta-sandwich capped by an alpha-helix) and binds to acidic phospholipids, suggesting a possible role in membrane localization.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Adaptor Proteins, Signal Transducing*
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Adaptor Proteins, Vesicular Transport*
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Amino Acid Sequence
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Binding Sites
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Blood Proteins / chemistry
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Ligands
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Magnetic Resonance Spectroscopy
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Models, Molecular
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Molecular Sequence Data
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Peptide Fragments / chemistry
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Peptide Fragments / metabolism
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Phospholipids / metabolism
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Phosphopeptides / chemistry
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Phosphopeptides / metabolism
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Phosphoproteins*
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Phosphotyrosine / metabolism*
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Protein Conformation
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Protein Structure, Secondary
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Proteins / chemistry*
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Proteins / metabolism
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Proto-Oncogene Proteins / chemistry
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Proto-Oncogene Proteins / metabolism
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Receptor Protein-Tyrosine Kinases / chemistry
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Receptor Protein-Tyrosine Kinases / metabolism
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Receptor, trkA
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Receptors, Nerve Growth Factor / chemistry
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Receptors, Nerve Growth Factor / metabolism
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Shc Signaling Adaptor Proteins
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Signal Transduction
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src Homology Domains
Substances
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Adaptor Proteins, Signal Transducing
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Adaptor Proteins, Vesicular Transport
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Blood Proteins
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Ligands
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Peptide Fragments
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Phospholipids
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Phosphopeptides
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Phosphoproteins
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Proteins
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Proto-Oncogene Proteins
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Receptors, Nerve Growth Factor
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Shc Signaling Adaptor Proteins
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platelet protein P47
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Phosphotyrosine
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Receptor Protein-Tyrosine Kinases
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Receptor, trkA