title: Crystal structure of the phosphotyrosine recognition domain SH2 of the Src oncogene product complexed with tyrosine-phosphorylated peptides.
abstract: SH2 domains are protein modules specialized in recognizing phosphorylated tyrosine residues and their sequence contexts. The mechanism of phosphotyrosine recognition and context recognition was elucidated in a series of X-ray crystallographic experiments which are discussed below.
authors.affiliation: Washington University School of Medicine, Department of Biochemistry and Molecular Biophysics, Saint-Louis, MO 63108.
authors.forename: G
authors.initials: G
authors.lastname: Waksman
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D003460:Crystallization; D018360:Crystallography, X-Ray; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D015394:Molecular Structure; D015513:Oncogene Proteins / Q000737:chemistry* / Q000378:metabolism; D010455:Peptides / Q000737:chemistry / Q000378:metabolism; D019000:Phosphotyrosine; D011485:Protein Binding; D017386:Sequence Homology, Amino Acid; D015398:Signal Transduction; D014443:Tyrosine / Q000031:analogs & derivatives* / Q000378:metabolism
chemical_list: D015513:Oncogene Proteins; D010455:Peptides; D019000:Phosphotyrosine; D014443:Tyrosine