Three-dimensional structure of the complexin/SNARE complex
Three-dimensional structure of the complexin/SNARE complex
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DOI：
10.1016/s0896-6273(02)00583-4
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发表时间：
2002-01-31
期刊：
影响因子：
16.2
通讯作者：
Rizo, J
中科院分区：
文献类型：
--
作者：
Chen, XC;Tomchick, DR;Rizo, J
在神经递质释放期间，神经元SNARE蛋白突触泡蛋白/VAMP、突触融合蛋白和SNAP-25形成四螺旋束，即SNARE复合物，其将突触囊泡和质膜拉在一起，可能导致膜融合。复合蛋白与SNARE复合物紧密结合，对于有效的Ca 2+诱发的神经递质释放至关重要。结合X射线和基于TROSY的NMR研究现在揭示了复合蛋白/SNARE复合物的原子结构。复合蛋白以反平行的α-螺旋构象结合到小突触泡蛋白和突触融合蛋白螺旋之间的凹槽。这种相互作用稳定了这两个螺旋之间的界面，该界面承受着并列膜之间的排斥力。这些结果表明，复合物稳定的完全组装的陷阱复合物作为一个关键步骤，使精致的高速度的Ca 2+诱发的神经递质释放。
During neurotransmitter release, the neuronal SNARE proteins synaptobrevin/VAMP, syntaxin, and SNAP-25 form a four-helix bundle, the SNARE complex, that pulls the synaptic vesicle and plasma membranes together possibly causing membrane fusion. Complexin binds tightly to the SNARE complex and is essential for efficient Ca2+-evoked neurotransmitter release. A combined X-ray and TROSY-based NMR study now reveals the atomic structure of the complexin/SNARE complex. Complexin binds in an antiparallel alpha-helical conformation to the groove between the synaptobrevin and syntaxin helices. This interaction stabilizes the interface between these two helices, which bears the repulsive forces between the apposed membranes. These results suggest that complexin stabilizes the fully assembled SNARE complex as a key step that enables the exquisitely high speed of Ca2+-evoked neurotransmitter release.