In silico Protein Structure Comparison of Conotoxins with VI/VII Cysteine Framework

TLDR: In silico structural models and alignments of ω-conotoxin and different pharmacological family with the same cysteine framework (VI/VII) will be discussed using computational methods -- FATCAT and POSA.

Abstract: Conopeptides are small disulfide-rich peptides isolated from the venom of marine cone snails, and they are amongst the most interesting of the venom species. In this paper, in silico structural models and alignments of ω-conotoxin and different pharmacological family with the same cysteine framework (VI/VII) will be discussed using computational methods -- FATCAT and POSA. The results show that with the ω-CTX conopeptide aligned with ω-CTX conopeptide, it would most likely have significantly similar structures with lower RMSD as they both function as blockers of voltage-gated calcium channels, and this conopeptide would be ω-CTX MVIIA 1OMGA aligned with ω-CTX MVIIA 1TTK. On the other hand, having compared different pharmacological with ω-CTX would result to a fewer significantly similar results since their amino acid residues, and ion channels are quite different. Multiple alignment of structures across different pharmacological families show similarities in their polypeptide backbone. Hence,conotoxins sharing the same cysteine framework can be used as models for deducing the polypeptide backbone of a conotoxin with unknown structure.