Abstract
Cone snails (Conus) elaborate a series of conotoxin (CTX) peptides in their venoms to paralyze their prey. Among these toxins, ω-CTX’s specifically target to presynaptic voltage-gated calcium channel subsets, causing inhibition of neurotransmitter release. ε-CTX SO3 was isolated from the venom ofConus striatus, which is the only available fish-hunting snail near the coast of the South China Sea. The three-dimensional solution structure of ω-CTX SO3, a peptide which is the only ω-conotoxin reported to show high homology with another ω-CTX (MVIIA fromC. Magus), has been determined by1H NMR techniques. The molecular structure of ω-CTX SO3 is stabilized by three disulfide bridges and a short triple-stranded antiparallel β-sheet with four turns. A comprehensive comparison suggested that the backbone conformation of ω-CTX’s was quite conserved, while the length of β-sheet and the type of some turns might have minor differences.
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Atomic coordinates for the 11 converged structures of ω-conotoxin SO3 have been deposited with the Protein Data Bank, Brookhaven National Laboratories, Long Island, NY 11973, under the accession code 1FYG.
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Yan, Y., Tu, G., Luo, X. et al. Three-dimensional solution structure of ω-conotoxin SO3 determined by1H NMR. Chin.Sci.Bull. 48, 1097–1102 (2003). https://doi.org/10.1007/BF03185760
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DOI: https://doi.org/10.1007/BF03185760