| Title: | Evidence for a C-terminal turn in PBAN. An NMR and distance geometry study |
| Address: | "Department of Chemistry, University at Stony Brook, New York, USA" |
| DOI: | 10.1111/j.1399-3011.1996.tb01085.x |
| ISSN/ISBN: | 0367-8377 (Print) 0367-8377 (Linking) |
| Abstract: | "The solution conformation of the pheromone biosynthesis activating neuropeptide (PBAN) of the moth Helicoverpa zea has been determined using homonuclear two-dimensional nuclear magnetic resonance techniques and distance geometry-restrained energy minimization. The insect peptide hormone showed a random distribution of conformers in aqueous solution, whereas in a less polar medium of trifluoroethanol and water, a reordering process was observed. In particular, the C-terminal region (Phe-Ser-Pro-Arg-Leu-NH2) adopts a type I' beta-turn conformation, residues 20-27 are in a helix conformation, and residues 1-19 exhibit a high degree of flexibility. Direct observation of the C-terminal beta-turn configuration of PBAN is consistent with a previous report that showed a rigid, cyclic analog of the C-terminal pentapeptide of PBAN retained pheromonotropic activity [Nachman, R.J., Kuniyoshi, H., Roberts, V.A., Holman, G.M. & Suzuki, A. (1993). Biochem. Biophys. Res. Commun. 661-666]. Furthermore, our results show no interaction between the C-terminal turn and the rest of the polypeptide chain, thus providing further evidence that the C-terminal turn is indeed the important conformation recognized by the PBAN receptor" |
| Keywords: | Amino Acid Sequence Animals Magnetic Resonance Spectroscopy Molecular Sequence Data Moths Neuropeptides/*chemistry Protein Conformation; |
| Notes: | "MedlineClark, B A Prestwich, G D eng AI32498/AI/NIAID NIH HHS/ RR05547A/RR/NCRR NIH HHS/ Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. Denmark 1996/05/01 Int J Pept Protein Res. 1996 May; 47(5):361-8. doi: 10.1111/j.1399-3011.1996.tb01085.x" |
