The pyrokinin/PBAN family of peptides and their receptors in Insecta: evolutionary trace indicates potential receptor ligand binding domains.

Russell A. Jurenka, Iowa State University
Tyasning Nusawardani, Iowa State University

This is a manuscript of an article in Insect Molecular Biology 20 (2011): 323, doi:10.1111/j.1365-2583.2010.01065.x. Posted with permission.


The pyrokinin/pheromone biosynthesis-activating neuropeptide (PBAN) family of G-protein-coupled receptors and their ligands have been identified in various insects. Physiological functions of pyrokinin peptides include muscle contraction, whereas PBAN regulates, among other functions, pheromone production in moths which indicates the pleiotropic nature of these peptides. Based on the alignment of annotated genomic sequences, the pyrokinin/PBAN family of receptors have similarity with the corresponding structures of the capa or periviscerokinins receptors of insects and the neuromedin U receptors of vertebrates. In our study, evolutionary trace (ET) analysis on the insect receptor sequences was conducted to predict the putative ligand recognition and binding sites. The ET analysis of four class-specific receptors indicated several amino acid residues that are conserved in the transmembrane domains. The receptor extracellular domains exhibit several classspecific amino acid residues, which could indicate putative domains for activation of these receptors by ligand recognition and binding.