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首页> 外文期刊>The Botulinum Journal >Comparison of the structural features of botulinum neurotoxin and NTNH, a non-toxic accessory protein of the progenitor complex
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Comparison of the structural features of botulinum neurotoxin and NTNH, a non-toxic accessory protein of the progenitor complex

机译：肉毒杆菌结构特点的比较神经毒素和NTNH无毒配件蛋白质的祖复杂

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摘要

The non-toxic, non-hemagglutinin (NTNH) protein occurs with the seven progenitor serotypes of the botulinum neurotoxins (BoNTs). Bioinformatic techniques predict that the N- and C-termini of NTNH have the same folds as the corresponding domains of BoNT. In contrast, the sequence pattern for zinc-binding in the catalytic domain of BoNT is absent in NTNH. The intermediate domain of NTNH is predicted to have neither the coiled-coil nor the hydrophobic characteristics of the corresponding region of BoNT.BoNT and NTNH are hypothesised to have diverged in their amino acid sequences from a common ancestor which accounts for their structural and functional differences.
机译：无毒,non-hemagglutinin (NTNH)的蛋白质发生的七祖种血清型肉毒神经毒素(肉毒毒素)。技术预测的N - c终端NTNH折叠为对应的相同肉毒毒素的域。模式的锌结合催化领域肉毒毒素是在NTNH缺席。域的NTNH是既没有预测卷曲螺旋和疏水特性相应的提升装置。提出有不同的氨基酸酸序列来自共同的祖先账户的结构和功能的差异。

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