Active conformation of the pyrokinin/PBAN neuropeptide family for pheromone biosynthesis in the silkworm.
Members of the pyrokinin/pheromone biosynthesis activating neuropeptide family elicit pheromonotropic activity in at least two species of moths. We report that in the silkworm (Bombyx mori) the conformationally constrained octapeptide analog cyclo[Asn-Thr-Ser-Phe-Thr-Pro-Arg-Leu] retains 10% of the pheromonotropic activity of naturally occurring Bom-PBAN-I, a 33 amino acid peptide. Previous data from CD, NMR, and molecular dynamics analyses indicate a type I beta-turn conformation for active core residues Thr-Pro-Arg-Leu in the cyclic analog. The rigidity of the well-defined backbone structure of this cyclic pyrokinin/PBAN analog suggests that it represents the conformation necessary to interact with the pheromonotropic receptor site in the silkworm.
Food Animal Protection Research Laboratory, U.S. Department of Agriculture, College Station, TX 77845.
R J
RJ
Nachman
H
H
Kuniyoshi
V A
VA
Roberts
G M
GM
Holman
A
A
Suzuki
D000595:Amino Acid Sequence; D000818:Animals; D012831:Bombyx; D007301:Insect Hormones / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009479:Neuropeptides / Q000737:chemistry*; D010456:Peptides, Cyclic / Q000737:chemistry*; D010675:Pheromones / Q000096:biosynthesis*; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid
D007301:Insect Hormones; D009479:Neuropeptides; D010456:Peptides, Cyclic; D010675:Pheromones; C079229:pyrokinin