PRIMARY STRUCTURE DETERMINATION AND CLONING OF THE CDNA-ENCODING TOXIN-4 OF THE SCORPION CENTRUROIDES-NOXIUS HOFFMANN

被引:24
作者
VAZQUEZ, A
BECERRIL, B
MARTIN, BM
ZAMUDIO, F
BOLIVAR, F
POSSANI, LD
机构
[1] UNIV NACL AUTONOMA MEXICO, INST BIOTECNOL, AV UNIV 2001, APTO POSTAL 5103, CUERNAVACA 62271, MEXICO
[2] NIMH, CLIN NEUROSCI BRANCH, MOLEC NEUROGENET UNIT, BETHESDA, MD 20892 USA
来源
FEBS LETTERS | 1993年 / 320卷 / 01期
关键词
SCORPION TOXIN; NA+CHANNEL; CDNA CLONE; NUCLEOTIDE SEQUENCE; PEPTIDE PROCESSING;
D O I
10.1016/0014-5793(93)81654-I
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:43 / 46
页数:4
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