1br0: Difference between revisions

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[[Image:1br0.gif|left|200px]]<br /><applet load="1br0" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1br0.gif|left|200px]]<br /><applet load="1br0" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1br0" />

'''THREE DIMENSIONAL STRUCTURE OF THE N-TERMINAL DOMAIN OF SYNTAXIN 1A'''<br />

==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.

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 [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].

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==

Line 16:

[[Category: Fernandez, I.]]

[[Category: Rizo, J.]]

[[Category: Sudhof, T.C.]]

[[Category: Sudhof, T C.]]

[[Category: Ubach, J.]]

[[Category: Zhang, X.]]

Line 24:

[[Category: syntaxin]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:58:09 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1br0.gif|left|200px]]<br /><applet load="1br0" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1br0.gif|left|200px]]<br /><applet load="1br0" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1br0" />
 '''THREE DIMENSIONAL STRUCTURE OF THE N-TERMINAL DOMAIN OF SYNTAXIN 1A'''<br />
 ==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.
+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==
-BR0 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].
+BR0 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==
@@ Line 16: / Line 16: @@
 [[Category: Fernandez, I.]]
 [[Category: Rizo, J.]]
-[[Category: Sudhof, T.C.]]
+[[Category: Sudhof, T C.]]
 [[Category: Ubach, J.]]
 [[Category: Zhang, X.]]
@@ Line 24: / Line 24: @@
 [[Category: syntaxin]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:50:52 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:58:09 2008''