AI Article Synopsis
- AlphaD-conotoxins, derived from the marine snail Conus vexillum, are identified as peptide inhibitors of nicotinic acetylcholine receptors (nAChRs) and are now renamed to alphaD-VxXXA, alphaD-VxXXB, and alphaD-VxXXC.
- Researchers reported cDNA sequences for D-superfamily conopeptides from various Conus species, revealing that the signal peptide sequences exhibit more diversity than other conotoxin families.
- Phylogenetic analysis shows two distinct groups based on signal peptide motifs, and combinations of peptide sequences contribute to understanding the structure and variability of these conotoxins across different Conus species.
Article Abstract
AlphaD-conotoxins are peptide inhibitors of nicotinic acetylcholine receptors (nAChRs) first described from Conus vexillum (alphaD-VxXIIA-C and renamed here to alphaD-VxXXA, alphaD-VxXXB, and alphaD-VxXXC). In this study, we report cDNA sequences encoding D-superfamily conopeptides identified in the Clade XII Conidae Conus vexillum, Conus capitaneus, Conus mustelinus, and Conus miles, together with partial sequences of corresponding peptides from this family. The D-superfamily signal peptide sequences display greater heterogeneity than reported for other conotoxin superfamilies. Phylogenetic analysis of the relationships among alphaD-conotoxin precursors reveals two distinct groups containing either an EMM or AVV signal peptide sequence motif. Homodimer and heterodimer combinations of predicted mature toxin sequences likely account for the partial amino acid sequences and mass values observed for several of the native dimeric peptide components identified in C. capitaneus, C. miles, and C. mustelinus venom. The discovery of the precursors and several novel conotoxins from different species defines this large conotoxin family and expands our understanding of sequence diversification mechanisms in Conus species.
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| http://dx.doi.org/10.1021/bi9000326 | DOI Listing |
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