3-DIMENSIONAL STRUCTURE OF NATURAL CHARYBDOTOXIN IN AQUEOUS-SOLUTION BY H-1-NMR - CHARYBDOTOXIN POSSESSES A STRUCTURAL MOTIF FOUND IN OTHER SCORPION TOXINS
3-DIMENSIONAL STRUCTURE OF NATURAL CHARYBDOTOXIN IN AQUEOUS-SOLUTION BY H-1-NMR - CHARYBDOTOXIN POSSESSES A STRUCTURAL MOTIF FOUND IN OTHER SCORPION TOXINS
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DOI：
10.1111/j.1432-1033.1991.tb15780.x
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发表时间：
1991-02-26
期刊：
影响因子：
--
通讯作者：
TOMA, F
中科院分区：
文献类型：
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作者：
BONTEMS, F;ROUMESTAND, C;TOMA, F
本文报道了作用于K ~+通道的天然蝎毒素的600 MHz质子核磁共振研究。实现了毒素的所有质子的明确的顺序分配。NOE和骨架偶联常数的分析表明，在26-35部分存在α-螺旋（残基10-19）和反平行β-折叠。通过距离几何生成三维结构，使用一组114个残差间校准约束（63个连续约束，47个中远程约束，4个氢键约束）和29个PHI角。这些结构表明，Charybdotoxin由通过两个二硫桥连接到α-螺旋和通过第三个二硫桥连接到延伸片段的β-折叠组成。与其他已知的长和短蝎毒素结构的比较表明，这种结构基序是共同的所有这些蛋白质。
A 600-MHz proton NMR study of natural charybdotoxin, a toxin acting on K+ channels, is reported. The unambiguous sequential assignment of all the protons of the toxin was achieved. The analysis of NOEs and of backbone coupling constants showed the existence of an alpha-helix (residues 10-19) and of an antiparallel beta-sheet in the 26-35 part. Three-dimensional structures were generated by distance geometry, using a set of 114 inter-residual calibrated constraints (63 sequential, 47 medium and long range, 4 hydrogen bonds) and 29 PHI-angles. These structures show that charybdotoxin is composed of a beta-sheet linked to an alpha-helix by two disulphide bridges and to an extended fragment by the third disulphide bridge. Comparison with the other known structures of long and short scorpion toxins shows that this structural motif is common to all these proteins.