title: Primary structure determination and cloning of the cDNA encoding toxin 4 of the scorpion Centruroides noxius Hoffmann.
abstract: A peptide (toxin II-10), shown to be a Na+ channel blocker, was purified from the venom of the scorpion Centruroides noxius Hoffmann and sequenced by Edman degradation. It has 66 amino acid residues with the C-terminal residue (asparagine) amidated, as demonstrated by mass spectrometry. In addition, we report the cloning and the nucleotide sequence of the cDNA (CngtV) that codes for this toxin. We discuss the mechanism for processing the precursor peptide to its final form and compare the primary structure to that of other Na+ channel toxins. Two distinct groups of toxins seem to emerge from this comparison, suggesting a structure-function relationship of these peptides towards the recognition of either mammalian or insect tissues.
authors: Instituto de Biotecnología, Universidad Nacional Autónoma de México, Cuernavaca.
authors: A
authors: A
authors: Vázquez
authors: B
authors: B
authors: Becerril
authors: B M
authors: BM
authors: Martin
authors: F
authors: F
authors: Zamudio
authors: F
authors: F
authors: Bolívar
authors: L D
authors: LD
authors: Possani
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D004247:DNA; D008969:Molecular Sequence Data; D011499:Protein Processing, Post-Translational; D012604:Scorpion Venoms / Q000737:chemistry* / Q000235:genetics; D012605:Scorpions; D017386:Sequence Homology, Amino Acid
chemical_list: D012604:Scorpion Venoms; C080517:toxin 4, Centruroides noxius; D004247:DNA