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  Arrangement of subunits in 20 s particles consisting of nsf, snaps, and snare complexes

Hohl, T. M., Parlati, F., Wimmer, C., Rothman, J. E., Söllner, T. H., & Engelhardt, H. (1998). Arrangement of subunits in 20 s particles consisting of nsf, snaps, and snare complexes. Molecular Cell, 2(5), 539-548.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-71E7-B Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-71E8-9
Genre: Journal Article

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Hohl, T. M., Author
Parlati, F., Author
Wimmer, C., Author
Rothman, J. E., Author
Söllner, T. H., Author
Engelhardt, H.1, Author              
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1External Organizations, ou_persistent22              

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Free keywords: Sensitive fusion protein; Synaptosomal-associated protein; Synaptic vesicle docking; Membrane-fusion; Vesicular transport; Alpha-snap; V-snare; Electron-microscopy; Mammalian-cells; Core complex.; Cell & developmental biology.
 Abstract: 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. [References: 61]

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 Dates: 1998-11
 Publication Status: Published in print
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 Rev. Method: -
 Identifiers: eDoc: 318320
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Title: Molecular Cell
Source Genre: Journal
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Pages: - Volume / Issue: 2 (5) Sequence Number: - Start / End Page: 539 - 548 Identifier: -