1l4a: Difference between revisions

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[[Image:1l4a.gif|left|200px]]<br /><applet load="1l4a" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1l4a.gif|left|200px]]<br /><applet load="1l4a" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1l4a, resolution 2.95Å" />

'''X-RAY STRUCTURE OF THE NEURONAL COMPLEXIN/SNARE COMPLEX FROM THE SQUID LOLIGO PEALEI'''<br />

==Overview==

Nerve terminals release neurotransmitters from vesicles into the synaptic, cleft upon transient increases in intracellular Ca(2+). This exocytotic, process requires the formation of trans SNARE complexes and is regulated, by accessory proteins including the complexins. Here we report the crystal, structure of a squid core complexin-SNARE complex at 2.95-A resolution. A, helical segment of complexin binds in anti-parallel fashion to the, four-helix bundle of the core SNARE complex and interacts at its C, terminus with syntaxin and synaptobrevin around the ionic zero layer of, the SNARE complex. We propose that this structure is part of a, multiprotein fusion machinery that regulates vesicle fusion at a late, pre-fusion stage. Accordingly, Ca(2+) may initiate membrane fusion by, acting directly or indirectly on complexin, thus allowing the, conformational transitions of the trans SNARE complex that are thought to, drive membrane fusion.

Nerve terminals release neurotransmitters from vesicles into the synaptic cleft upon transient increases in intracellular Ca(2+). This exocytotic process requires the formation of trans SNARE complexes and is regulated by accessory proteins including the complexins. Here we report the crystal structure of a squid core complexin-SNARE complex at 2.95-A resolution. A helical segment of complexin binds in anti-parallel fashion to the four-helix bundle of the core SNARE complex and interacts at its C terminus with syntaxin and synaptobrevin around the ionic zero layer of the SNARE complex. We propose that this structure is part of a multiprotein fusion machinery that regulates vesicle fusion at a late pre-fusion stage. Accordingly, Ca(2+) may initiate membrane fusion by acting directly or indirectly on complexin, thus allowing the conformational transitions of the trans SNARE complex that are thought to drive membrane fusion.

==About this Structure==

1L4A is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Loligo_plei Loligo plei]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1L4A OCA].

1L4A is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Loligo_plei Loligo plei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L4A OCA].

==Reference==

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[[Category: snare complex]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20 20~~:14:~~46 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:41:10 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1l4a.gif|left|200px]]<br /><applet load="1l4a" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1l4a.gif|left|200px]]<br /><applet load="1l4a" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1l4a, resolution 2.95&Aring;" />
 '''X-RAY STRUCTURE OF THE NEURONAL COMPLEXIN/SNARE COMPLEX FROM THE SQUID LOLIGO PEALEI'''<br />
 ==Overview==
-Nerve terminals release neurotransmitters from vesicles into the synaptic, cleft upon transient increases in intracellular Ca(2+). This exocytotic, process requires the formation of trans SNARE complexes and is regulated, by accessory proteins including the complexins. Here we report the crystal, structure of a squid core complexin-SNARE complex at 2.95-A resolution. A, helical segment of complexin binds in anti-parallel fashion to the, four-helix bundle of the core SNARE complex and interacts at its C, terminus with syntaxin and synaptobrevin around the ionic zero layer of, the SNARE complex. We propose that this structure is part of a, multiprotein fusion machinery that regulates vesicle fusion at a late, pre-fusion stage. Accordingly, Ca(2+) may initiate membrane fusion by, acting directly or indirectly on complexin, thus allowing the, conformational transitions of the trans SNARE complex that are thought to, drive membrane fusion.
+Nerve terminals release neurotransmitters from vesicles into the synaptic cleft upon transient increases in intracellular Ca(2+). This exocytotic process requires the formation of trans SNARE complexes and is regulated by accessory proteins including the complexins. Here we report the crystal structure of a squid core complexin-SNARE complex at 2.95-A resolution. A helical segment of complexin binds in anti-parallel fashion to the four-helix bundle of the core SNARE complex and interacts at its C terminus with syntaxin and synaptobrevin around the ionic zero layer of the SNARE complex. We propose that this structure is part of a multiprotein fusion machinery that regulates vesicle fusion at a late pre-fusion stage. Accordingly, Ca(2+) may initiate membrane fusion by acting directly or indirectly on complexin, thus allowing the conformational transitions of the trans SNARE complex that are thought to drive membrane fusion.
 ==About this Structure==
-L4A is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Loligo_plei Loligo plei]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1L4A OCA].
+L4A is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Loligo_plei Loligo plei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L4A OCA].
 ==Reference==
@@ Line 22: / Line 22: @@
 [[Category: snare complex]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:14:46 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:41:10 2008''