New insights into clostridial neurotoxin-SNARE interactions

被引：55

作者：

Breidenbach, MA

Brunger, AT ^{[1
]}

机构：

[1] Stanford Univ, Howard Hughes Med Inst, Stanford, CA 94305 USA

[2] Stanford Univ, Dept Cellular & Mol Physiol, Stanford, CA 94305 USA

[3] Stanford Univ, Dept Neurol & Neurol Sci, Stanford, CA 94305 USA

[4] Stanford Univ, Stanford Synchrotron Radiat Lab, Stanford, CA 94305 USA

来源：

TRENDS IN MOLECULAR MEDICINE | 2005年 / 11卷 / 08期

关键词：

D O I：

10.1016/j.molmed.2005.06.012

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：

Botulinum neurotoxin serotype A (BoNT/A) has achieved a dichotomous status in modern medicine; it is both a versatile treatment for several neurological disorders and a lethal poison responsible for causing the neuroparalytic syndrome botulism. The extent of paralysis largely depends on the dosage of toxin received. The toxins block neurotransmitter release by delivering their Zn2+-dependent protease components to the presynaptic side of chemical synapses. These highly specialized enzymes exclusively hydrolyze peptide bonds within SNARE (soluble N-ethylmaleiamidesensitive factor attachment protein receptor) proteins. Recently, the structural basis for the highly specific interaction between BoNT/A and its target SNARE, SNAP-25 (synaptosomal-associated protein of 25 kDa), was elucidated. Now details regarding the nature of the toxin-SNARE interactions could be exploited for novel inhibitor design.

引用

页码：377 / 381

页数：5

共 70 条

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