神经元t-SNARE复合体是一个平行的四螺旋束。

The neuronal t-SNARE complex is a parallel four-helix bundle.

作者信息

Xiao W, Poirier M A, Bennett M K, Shin Y K

机构信息

Department of Chemistry, University of California, Berkeley, California 94720, USA.

出版信息

Nat Struct Biol. 2001 Apr;8(4):308-11. doi: 10.1038/86174.

DOI:10.1038/86174

PMID:11276248

Abstract

Assembly of the soluble N-ethylmaleimide sensitive factor attachment protein receptor (SNARE) complex is an essential step for neurotransmitter release in synapses. The presynaptic plasma membrane associated proteins (t-SNAREs), SNAP-25 (synaptosome-associated protein of 25,000 Da) and syntaxin 1A may form an intermediate complex that later binds to vesicle-associated membrane protein 2 (VAMP2). Using spin labeling electron paramagnetic resonance (EPR), we found that the two t-SNARE proteins assemble into a parallel four-helix bundle that consists of two identical syntaxin 1A components and the N-terminal and C-terminal domains of SNAP-25. Although the structure is generally similar to that of the final SNARE complex, the middle region of the helical bundle appears more flexible in the t-SNARE complex. Such flexibility might facilitate interactions between VAMP2 and the t-SNARE complex.

摘要

可溶性N - 乙基马来酰亚胺敏感因子附着蛋白受体（SNARE）复合物的组装是突触中神经递质释放的关键步骤。突触前质膜相关蛋白（t - SNAREs），SNAP - 25（25000 Da的突触体相关蛋白）和 syntaxin 1A可能形成一种中间复合物，该复合物随后与囊泡相关膜蛋白2（VAMP2）结合。使用自旋标记电子顺磁共振（EPR），我们发现这两种t - SNARE蛋白组装成一个平行的四螺旋束，该四螺旋束由两个相同的syntaxin 1A组件以及SNAP - 25的N端和C端结构域组成。尽管该结构总体上与最终的SNARE复合物相似，但在t - SNARE复合物中螺旋束的中间区域显得更具灵活性。这种灵活性可能有助于VAMP2与t - SNARE复合物之间的相互作用。