Conserved molecular switch interactions in modeled cardioactive RF-NH2 peptide receptors: Ligand binding and activation.

摘要: Peptides may act through G protein-coupled receptors to influence cardiovascular performance; thus, delineating mechanisms involved in signaling is a molecular-based strategy health. Molecular switches, often represented by conserved motifs, maintain receptor an inactive state. However, once the switch broken, transmembrane regions move and activation occurs. The molecular switches of Drosophila melanogaster myosuppressin (MS) were previously identified include unique ionic lock novel 3-6 lock, as well transmission tyrosine toggle switches. In addition MS, cardioactive ligands structurally related C-terminal RF-NH2 sulfakinin, neuropeptide F (NPF), short NPF, FMRF-NH2-containing peptide subfamilies. We hypothesized motifs within subfamily across species. Thus, we investigated (RFa-R) D. melanogaster, Tribolium castaneum, Anopheles gambiae, Rhodnius prolixus, Bombyx mori. Adipokinetic hormone (AKH), which does not contain RF-NH2, was also examined. showed higher degree conservation than 3-7 lock. AKH representative subfamily. interactions RFa-Rs consistent with ligand-specific binding.