1sfc
From Proteopedia
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NEURONAL SYNAPTIC FUSION COMPLEX
Overview
The evolutionarily conserved SNARE proteins and their complexes are, involved in the fusion of vesicles with their target membranes; however, the overall organization and structural details of these complexes are, unknown. Here we report the X-ray crystal structure at 2.4 A resolution of, a core synaptic fusion complex containing syntaxin-1 A, synaptobrevin-II, and SNAP-25B. The structure reveals a highly twisted and parallel, four-helix bundle that differs from the bundles described for the, haemagglutinin and HIV/SIV gp41 membrane-fusion proteins. Conserved, leucine-zipper-like layers are found at the centre of the synaptic fusion, complex. Embedded within these leucine-zipper layers is an ionic layer, consisting of an arginine and three glutamine residues contributed from, each of the four alpha-helices. These residues are highly conserved across, the entire SNARE family. The regions flanking the leucine-zipper-like, layers contain a hydrophobic core similar to that of more general, four-helix-bundle proteins. The surface of the synaptic fusion complex is, highly grooved and possesses distinct hydrophilic, hydrophobic and charged, regions. These characteristics may be important for membrane fusion and, for the binding of regulatory factors affecting neurotransmission.
About this Structure
1SFC is a Protein complex structure of sequences from Rattus norvegicus with SR and MPD as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution., Sutton RB, Fasshauer D, Jahn R, Brunger AT, Nature. 1998 Sep 24;395(6700):347-53. PMID:9759724
Page seeded by OCA on Wed Nov 21 02:20:34 2007
