The structure of the amino terminal transforming segment of the p21 protein, Tyr4-Thr20 (with Asp12), by two-dimensional NMR.
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.
Longo
P A
PA
Dept. of Chemistry, Hunter College, New York, NY.
Broido
M S
MS
Chen
J
J
Kung
H F
HF
Pincus
M R
MR
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*
D009842:Oligopeptides; D011518:Proto-Oncogene Proteins; D019204:GTP-Binding Proteins