Three-dimensional solution structure of the src homology 2 domain of c-abl.
SH2 regions are protein motifs capable of binding target protein sequences that contain a phosphotyrosine. The solution structure of the abl SH2 product, a protein of 109 residues and 12.1 kd, has been determined by multidimensional nuclear magnetic resonance spectroscopy. It is a compact spherical domain with a pair of three-stranded antiparallel beta sheets and a C-terminal alpha helix enclosing the hydrophobic core. Three arginines project from a short N-terminal alpha helix and one beta sheet into the putative phosphotyrosine-binding site, which lies on a face distal from the termini. Comparison with other SH2 sequences supports a common global fold and mode of phosphotyrosine binding for this family.
Overduin
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Laboratories of The Rockefeller University New York, New York 10021.
Rios
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Mayer
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Baltimore
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Cowburn
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D000595:Amino Acid Sequence; D016313:Genes, abl; D016391:Genes, src; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D011506:Proteins / Q000737:chemistry*; D016415:Sequence Alignment
D011506:Proteins