Structure-function relationship of clostridial neurotoxins
Structure-function relationship of clostridial neurotoxins
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DOI：
10.3109/15569549909036019
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发表时间：
1999-01-01
期刊：
影响因子：
--
通讯作者：
Singh, BR
中科院分区：
文献类型：
--
作者：
Li, L;Singh, BR
肉毒神经毒素是一类独特的金属蛋白酶，它催化参与突触囊泡与质膜对接和融合以释放神经递质的特定蛋白质的单位点切割。7种血清型肉毒毒素具有共同的分子作用模式，但在一级氨基酸序列和作用于神经细胞的蛋白质底物上存在显著差异。神经毒素是大的水溶性蛋白质（150 kDa），具有不同的结构域，在毒物发生过程中与不同的生化功能相关。在这篇综述中，我们重点描述了特定蛋白片段在毒素分子的结合、转运和内肽酶活性中的作用。
Botulinum neurotoxins are a unique group of metalloproteases which catalyze single site cleavage of specific proteins involved in the docking and fusion off synaptic vesicles with plasma membrane for neurotransmitter release. Seven serotypes of botulinum neurotoxins share a common molecular mode of action, with remarkable difference in their primary amino acid sequences and protein substrates in neuronal cells. The neurotoxins are large water soluble proteins (150 kDa) with distinct domains associated with different biochemical functions during the toxicogenesis process. In this review, we have focused on the description of the role of specific protein segments in the binding, translocation and endopeptidase activity of the toxin molecules.