Maurotoxin, a four disulfide bridge toxin from Scorpio maurus venom: Purification, structure and action on potassium channels

被引:91
作者
Kharrat, R
Mansuelle, P
Sampieri, F
Crest, M
Oughideni, R
VanRietschoten, J
MartinEauclaire, MF
Rochat, H
ElAyeb, M
机构
[1] UNIV MEDITERRANEE, UMR 6560,CNRS,LAB BIOCHIM INGN PROT,IFR JEAN ROCHE, FAC MED NORD, F-13916 MARSEILLE 20, FRANCE
[2] NEUROBIOL LAB, CNRS, UPR 9024, F-13402 MARSEILLE, FRANCE
关键词
scorpion toxin; potassium channel;
D O I
10.1016/S0014-5793(97)00285-8
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 new toxin acting on K+ channels, maurotoxin (MTX), has been purified to homogeneity from the venom of the chactoid scorpion Scorpio maurus. MTX is a basic single chain 34 amino acid residue polypeptide, amidated at its C terminal, and crosslinked by four disulfide bridges, It shows 29-68% sequence identity with other K+ channel toxins, and presents an original disulfide pattern, the last two half-cystine residues (31-34) being connected, Although the first three disulfide bonds hare not been defined experimentally, modelling based on the structure of charybdotoxin favored two combinations out of six, one of which has two bridges (3-24 and 9-29) in common with the general motif of scorpion toxins, The last bridge would connect residues 13 and 19. MTX inhibits the binding to Eat brain synaptosomal membranes of both [I-125]apamin, a SKCa channel blocker (IC50 5 nM), and [I-125]kaliotoxin, a Kv channel blocker (IC50 30 pM). MTX blocks the Kv1.1, Kv1.2 and Kv1.3 currents expressed in Xenopus oocytes with IC50 of 45, 0.8 and 180 nM, respectively, MTX represents a member of a new class of short toxins with 4 disulfide bridges, active on voltage-dependent K+ channel and also competing with apamin for binding to its receptor. (C) 1997 Federation of European Biochemical Societies.
引用
收藏
页码:284 / 290
页数:7
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