An oligopeptide containing the C-terminal sequence of RNase a has a potent RNase a binding property.
We demonstrate that an oligopeptide containing the C-terminal sequence of RNase A binds to RNase A in a stoichiometric and site-specific manner. Our observations are consistent with the interaction found in the major domain-swapped RNase A dimer, so that the peptide binding may be promoted through the swapping with the C-terminal beta-sheet of RNase A. Because the design of a protein-binding peptide is much simpler than other methods such as the combinatorial method, we propose that investigation using an oligopeptide may be of general application to domain swapping in proteins as well as for the development of an oligopeptide tool that specifically binds to a target protein.
Nakano
Shu-Ichi
S
Department of Chemistry, Faculty of Science and Engineering, Konan University, 8-9-1 Okamoto, Higashinada-ku, Kobe 658-8501, Japan.
Sugimoto
Naoki
N
D000595:Amino Acid Sequence; D005456:Fluorescent Dyes / Q000737:chemistry; D007700:Kinetics; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000138:chemical synthesis / Q000737:chemistry* / Q000378:metabolism*; D011485:Protein Binding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D012259:Ribonuclease, Pancreatic / Q000737:chemistry* / Q000378:metabolism*; D013053:Spectrophotometry
D005456:Fluorescent Dyes; D009842:Oligopeptides; D012259:Ribonuclease, Pancreatic