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Primary structure determination and cloning of the cDNA encoding toxin 4 of the scorpion Centruroides noxius Hoffmann
Author(s) -
Vázquez A.,
Becerril B.,
Martin B.M.,
Zamudio F.,
Bolívar F.,
Possani L.D.
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)81654-i
Subject(s) - edman degradation , venom , toxin , protein primary structure , complementary dna , scorpion toxin , peptide , peptide sequence , microbiology and biotechnology , biology , amino acid , biochemistry , chemistry , scorpion , gene
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.