1br0
| |||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THREE DIMENSIONAL STRUCTURE OF THE N-TERMINAL DOMAIN OF SYNTAXIN 1A
OverviewOverview
Syntaxin 1A plays a central role in neurotransmitter release through multiple protein-protein interactions. We have used NMR spectroscopy to identify an autonomously folded N-terminal domain in syntaxin 1A and to elucidate its three-dimensional structure. This 120-residue N-terminal domain is conserved in plasma membrane syntaxins but not in other syntaxins, indicating a specific role in exocytosis. The domain contains three long alpha helices that form an up-and-down bundle with a left-handed twist. A striking residue conservation is observed throughout a long groove that is likely to provide a specific surface for protein-protein interactions. A highly acidic region binds to the C2A domain of synaptotagmin I in a Ca2+-dependent interaction that may serve as an electrostatic switch in neurotransmitter release.
About this StructureAbout this Structure
1BR0 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
ReferenceReference
Three-dimensional structure of an evolutionarily conserved N-terminal domain of syntaxin 1A., Fernandez I, Ubach J, Dulubova I, Zhang X, Sudhof TC, Rizo J, Cell. 1998 Sep 18;94(6):841-9. PMID:9753330
Page seeded by OCA on Thu Mar 20 10:14:35 2008