Hohl T M, Parlati F, Wimmer C, Rothman J E, Söllner T H, Engelhardt H
Cellular Biochemistry and Biophysics Program, Memorial Sloan-Kettering Cancer Center, New York, New York 10021, USA.
Mol Cell. 1998 Nov;2(5):539-48. doi: 10.1016/s1097-2765(00)80153-7.
The structure of 20 S particles, consisting of NSF, SNAPs, and SNARE complexes, was analyzed by electron microscopy and fluorescence resonance energy transfer. Structural changes associated with the binding of alpha-SNAP and NSF to SNARE complexes define the contribution of each component to the 20 S particle structure. The synaptic SNARE complex forms a 2.5 x 15 nm rod. alpha-SNAP binds laterally to the rod, increasing its width but not its length. NSF binds to one end of the SNAP/SNARE complex; the resulting 20 S particles measure 22 nm in length and vary in width from 6 nm at their narrowest point to 13.5 nm at their widest. The transmembrane domains of VAMP and syntaxin emerge together at the NSF-distal end of 20 S particles, adjacent to the amino terminus of alpha-SNAP.
由N-乙基马来酰亚胺敏感因子（NSF）、可溶性NSF附着蛋白（SNAPs）和SNARE复合体组成的20S颗粒结构，通过电子显微镜和荧光共振能量转移进行了分析。与α-SNAP和NSF与SNARE复合体结合相关的结构变化，确定了每个组分对20S颗粒结构的贡献。突触SNARE复合体形成一个2.5×15纳米的杆状结构。α-SNAP横向结合到杆状结构上，增加其宽度但不增加长度。NSF结合到SNAP/SNARE复合体的一端；形成的20S颗粒长度为22纳米，宽度在最窄处为6纳米，最宽处为13.5纳米。囊泡相关膜蛋白（VAMP）和突触融合蛋白的跨膜结构域在20S颗粒的NSF远端共同出现，与α-SNAP的氨基末端相邻。
