2bu0 | pdb_00002bu0

MOLECULAR MODEL OF THE SYNAPTIC SNARE COMPLEX, CONSISTING OF THE SYNAPTIC VESICLE PROTEIN VAMP2 AND PRESYNAPTIC PLASMA MEMBRANE PROTEINS SNAP-25 AND SYNTAXIN 1A, EPR STUDY AND MODELING

spinqualitylabelsall models 2bu0 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, PDBsum Publication Abstract from PubMed The heterotrimeric synaptic soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complex, consisting of the synaptic vesicle-associated membrane protein 2 (VAMP2) and presynaptic plasma membrane proteins SNAP-25 (synaptosome-associated protein of 25,000 Mr) and syntaxin 1A, is a critical component of the exocytotic machinery. We have used spin labeling electron paramagnetic resonance spectroscopy to investigate the structural organization of this complex, particularly the two predicted helical domains contributed by SNAP-25. Our results indicate that the N- and C-terminal domains of SNAP-25 are parallel to each other and to the C-terminal domain of syntaxin 1A. Based on these findings, we propose a parallel four-stranded coiled coil model for the structure of the synaptic SNARE complex. The synaptic SNARE complex is a parallel four-stranded helical bundle.,Poirier MA, Xiao W, Macosko JC, Chan C, Shin YK, Bennett MK Nat Struct Biol. 1998 Sep;5(9):765-9. PMID:9731768 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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