1br0
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(New page: 200px<br /><applet load="1br0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1br0" /> '''THREE DIMENSIONAL STRUCTURE OF THE N-TERMINA...)
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Revision as of 09:43, 20 November 2007
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THREE DIMENSIONAL STRUCTURE OF THE N-TERMINAL DOMAIN OF SYNTAXIN 1A
Overview
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 Structure
1BR0 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
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
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