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• W2120405274 abstract "Syntaxin, vesicle-associated membrane protein (VAMP), and synaptosome-associated protein of 25 kDa (SNAP-25) form a ternary core complex central to the process of synaptic vesicle docking and fusion. Several lines of evidence support the hypothesis that the proteins assemble in a coiled-coil structure, but the alignment of alpha helices in this coil and the overall conformation of the coil are unknown. We employ the technique of fluorescence resonance energy transfer (FRET) to investigate the alignment between syntaxin and VAMP. With the acceptor probe coupled to the amino-terminal end of the VAMP coiled-coil domain, the donor probe fluorescence is quenched to a greater extent when it is on the amino-terminal end of the syntaxin H3 domain than when it is on the carboxy-terminal end. The data indicate that syntaxin and VAMP bind primarily in a parallel arrangement and suggest a coiled-coil structure that is bent rather than fully extended. We propose a model in which binding of SNAP receptor (SNARE) protein coiled-coil domains helps drive vesicle fusion." @default.
• W2120405274 created "2016-06-24" @default.
• W2120405274 creator A5007704434 @default.
• W2120405274 creator A5081487739 @default.
• W2120405274 date "1997-11-01" @default.
• W2120405274 modified "2023-10-14" @default.
• W2120405274 title "Structural Organization of the Synaptic Exocytosis Core Complex" @default.
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• W2120405274 doi "https://doi.org/10.1016/s0896-6273(00)80399-2" @default.
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