Primary structure determination and cloning of the cDNA encoding toxin 4 of the scorpion Centruroides noxius Hoffmann

FEBS Letters

Martin, B.M.¹  Vázquez, A.²  Zamudio, F.²  Becerril, B.²  Possani, L.D.²  Bolívar, F.² 

[1] National Institute of Mental Health, Molecular Neurogenetics Unit, Clinical Neuroscience Branch, Building 10 3N256 Bethesda, MD 20892, USA;Instituto de Biotecnologia, Universidad Nacional Autónoma de M'exico, Av. Universidad 2001, Cuernavaca 62271, México

关键词: Scorpion toxin;    Na−channel;    cDNA clone;    Nucleotide sequence;    Peptide processing;   

DOI  :  10.1016/0014-5793(93)81654-I

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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.

【 授权许可】

Unknown