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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[[Image:1br0.gif|left|200px]]<br /><applet load="1br0" size="350" color="white" frame="true" align="right" spinBox="true"
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'''THREE DIMENSIONAL STRUCTURE OF THE N-TERMINAL DOMAIN OF SYNTAXIN 1A'''<br />
'''THREE DIMENSIONAL STRUCTURE OF THE N-TERMINAL DOMAIN OF SYNTAXIN 1A'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1BR0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BR0 OCA].
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1BR0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BR0 OCA].
==Reference==
==Reference==
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[[Category: Fernandez, I.]]
[[Category: Fernandez, I.]]
[[Category: Rizo, J.]]
[[Category: Rizo, J.]]
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[[Category: Sudhof, T.C.]]
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[[Category: Sudhof, T C.]]
[[Category: Ubach, J.]]
[[Category: Ubach, J.]]
[[Category: Zhang, X.]]
[[Category: Zhang, X.]]
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[[Category: syntaxin]]
[[Category: syntaxin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:50:52 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:58:09 2008''

Revision as of 09:58, 21 February 2008


1br0

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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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