title: The structure of the amino terminal transforming segment of the p21 protein, Tyr4-Thr20 (with Asp12), by two-dimensional NMR.
abstract: The structure of a peptide from the transforming region (residues 4-20) of the p21 protein has been determined using two-dimensional NMR. In the normal protein, this segment contains a Gly residue at the critical 12 position; any substitution, other than Pro, at this position results in a transforming protein. Previously performed energy calculations indicated that this peptide segment is a structured one. In this study we find that the Asp12 containing peptide has a surprisingly well-defined structure in solution which has more similarity to the GDP-binding loop region in EF-tu than to that in p21.
authors.affiliation: Dept. of Chemistry, Hunter College, New York, NY.
authors.forename: P A
authors.initials: PA
authors.lastname: Longo
authors.forename: M S
authors.initials: MS
authors.lastname: Broido
authors.forename: J
authors.initials: J
authors.lastname: Chen
authors.forename: H F
authors.initials: HF
authors.lastname: Kung
authors.forename: M R
authors.initials: MR
authors.lastname: Pincus
mesh_terms: D000595:Amino Acid Sequence; D019204:GTP-Binding Proteins / Q000648:ultrastructure*; D011905:Genes, ras; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D009842:Oligopeptides; D011487:Protein Conformation; D011518:Proto-Oncogene Proteins / Q000648:ultrastructure*
chemical_list: D009842:Oligopeptides; D011518:Proto-Oncogene Proteins; D019204:GTP-Binding Proteins