Refined structure of charybdotoxin: common motifs in scorpion toxins and insect defensins
作者： F Bontems , C Roumestand , B Gilquin , A Menez , F Toma
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摘要: Conflicting three-dimensional structures of charybdotoxin (Chtx), a blocker K+ channels, have been previously reported. A high-resolution model depicting the tertiary structure Chtx has obtained by DIANA and X-PLOR calculations from new proton nuclear magnetic resonance (NMR) data. The protein possesses small triple-stranded antiparallel beta sheet linked to short helix two disulfides an extended fragment one disulfide, respectively. This motif also exists in all known scorpion toxins, irrespective their size, sequence, function. Strikingly, antibacterial insect defensins adopt this folding pattern.
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harvard.edu参考文章(18)
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