Characterization of a new peptide from Tityus serrulatus scorpion venom which is a ligand of the apamin‐binding site

FEBS Letters

Oughuideni, Razika²  Bougis, Pierre E.²  Darbon, Hervé¹  Rochat, Hervé²  Martin-Eauclaire, Marie-France²  Legros, Christian² 

[1] Architecture et fonction des Macromolécules Biologiques, UPR-9039, I.F.R.C.1 Institut Fédératif de Recherche du Centre National de la Recherche Scientifique, URA 1296, Chemin Joseph Aiguier, 13008 Marseille, France;Laboratoire de Biochimie, Ingénierie des Protéines, URA 1455 du Centre National de la Recherche Scientifique, Institut Fédératif Jean Roche, Faculté Médecine Nord, Boulevard Pierre Dramard, 13916 Marseille Cedex 20, France

关键词: Scorpion toxin;    cDNA;    Amino acid sequence;    Apamin;    Potassium channels;   

DOI  :  10.1016/0014-5793(96)00616-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A new ligand (Ts κ) of the apamin binding site on rat brain synaptosomes (K _0.5 = 300 pM) was purified and characterized from the venom of Tityus serrulatus. It is a polypeptide toxin of 35 amino acid residues, with three disulfide bridges. Its cDNA was amplified from a venom gland cDNA library and the nucleotide sequence determined. A model of Ts κ was constructed by amino acid replacement using charybdotoxin structure as determined by ¹H nuclear magnetic resonance as starting model.

【 授权许可】

Unknown