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Structure and ligand recognition of the phosphotyrosine binding domain of Shc.
- Source :
-
Nature [Nature] 1995 Dec 07; Vol. 378 (6557), pp. 584-92. - Publication Year :
- 1995
-
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.
- Subjects :
- Amino Acid Sequence
Binding Sites
Blood Proteins chemistry
Ligands
Magnetic Resonance Spectroscopy
Models, Molecular
Molecular Sequence Data
Peptide Fragments chemistry
Peptide Fragments metabolism
Phospholipids metabolism
Phosphopeptides chemistry
Phosphopeptides metabolism
Protein Conformation
Protein Structure, Secondary
Proteins metabolism
Proto-Oncogene Proteins chemistry
Proto-Oncogene Proteins metabolism
Receptor Protein-Tyrosine Kinases chemistry
Receptor Protein-Tyrosine Kinases metabolism
Receptor, trkA
Receptors, Nerve Growth Factor chemistry
Receptors, Nerve Growth Factor metabolism
Shc Signaling Adaptor Proteins
Signal Transduction
src Homology Domains
Adaptor Proteins, Signal Transducing
Adaptor Proteins, Vesicular Transport
Phosphoproteins
Phosphotyrosine metabolism
Proteins chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 0028-0836
- Volume :
- 378
- Issue :
- 6557
- Database :
- MEDLINE
- Journal :
- Nature
- Publication Type :
- Academic Journal
- Accession number :
- 8524391
- Full Text :
- https://doi.org/10.1038/378584a0