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.
Nachman
R J
RJ
Food Animal Protection Research Laboratory, U.S. Department of Agriculture, College Station, TX 77845.
Kuniyoshi
H
H
Roberts
V A
VA
Holman
G M
GM
Suzuki
A
A
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