NMR analysis of the structure of synaptobrevin and of its interaction with syntaxin
NMR analysis of the structure of synaptobrevin and of its interaction with syntaxin
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DOI：
10.1023/a:1008382027065
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发表时间：
1999-07-01
影响因子：
2.7
通讯作者：
Rizo, J
中科院分区：
文献类型：
--
作者：
Hazzard, J;S端dhof, TC;Rizo, J
Synaptobrevin是一种突触囊泡蛋白，在胞吐作用中起重要作用，并与Synaxin和SNAP-25形成SNARE复合体。我们用核磁共振波谱分析了分离的突触素的结构及其与突触素的二元相互作用。我们的结果表明，分离的突触短缩蛋白在溶液中大部分是展开的。Synaptobrevin的整个SNAR基序能够与分离的Synaxin的C末端SNAR基序相互作用，但只有少数残基与Synaxin的全长细胞质区域结合。这一结果表明Synaxin的N-末端和C-末端区域之间存在相互作用，与核心复合体组装竞争。
Synaptobrevin is a synaptic vesicle protein that has an essential role in exocytosis and forms the SNARE complex with syntaxin and SNAP-25. We have analyzed the structure of isolated synaptobrevin and its binary interaction with syntaxin using NMR spectroscopy. Our results demonstrate that isolated synaptobrevin is largely unfolded in solution. The entire SNARE motif of synaptobrevin is capable of interacting with the isolated C-terminal SNARE motif of syntaxin but only a few residues bind to the full-length cytoplasmic region of syntaxin. This result suggests an interaction between the N- and C-terminal regions of syntaxin that competes with core complex assembly.