Arrangement of subunits in 20 S particles consisting of NSF, SNAPs, and SNARE complexes

作者：Hohl TM; Parlati F; Wimmer C; Rothman JE; Sollner TH^*; Engelhardt H

来源：Molecular Cell, 1998, 2(5): 539-548.

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.

• 出版日期1998-11