title: Three-dimensional solution structure of the src homology 2 domain of c-abl.
abstract: 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.
authors.affiliation: Laboratories of The Rockefeller University New York, New York 10021.
authors.forename: M
authors.initials: M
authors.lastname: Overduin
authors.forename: C B
authors.initials: CB
authors.lastname: Rios
authors.forename: B J
authors.initials: BJ
authors.lastname: Mayer
authors.forename: D
authors.initials: D
authors.lastname: Baltimore
authors.forename: D
authors.initials: D
authors.lastname: Cowburn
mesh_terms: 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
chemical_list: D011506:Proteins