1fvf
From Proteopedia
(New page: 200px<br /><applet load="1fvf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fvf, resolution 3.2Å" /> '''CRYSTAL STRUCTURE ANA...) |
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| - | [[Image:1fvf.gif|left|200px]]<br /><applet load="1fvf" size=" | + | [[Image:1fvf.gif|left|200px]]<br /><applet load="1fvf" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1fvf, resolution 3.2Å" /> | caption="1fvf, resolution 3.2Å" /> | ||
'''CRYSTAL STRUCTURE ANALYSIS OF NEURONAL SEC1 FROM THE SQUID L. PEALEI'''<br /> | '''CRYSTAL STRUCTURE ANALYSIS OF NEURONAL SEC1 FROM THE SQUID L. PEALEI'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Sec1 molecules associate with t-SNAREs from the syntaxin family in a | + | Sec1 molecules associate with t-SNAREs from the syntaxin family in a heterodimeric complex that plays an essential role in vesicle transport and membrane fusion. Neuronal rat n-Sec1 has an arch-shaped three-domain structure, which binds syntaxin 1a through contacts in domains 1 and 3. In both rat nSec1 and homologous squid s-Sec1, a potential effector-molecule binding-pocket is shaped by residues from domains 1 and 2 and is localized on the opposite side of the syntaxin 1a interaction site. Comparison of several crystal forms of unliganded neuronal squid Sec1 indicates a hinge region between domains 1 and 2 which allows domain 1 to rotate along a central axis. This movement could release syntaxin 1a upon interaction with a yet unspecified Sec1 effector molecule(s). The binding of an effector protein may also directly affect the conformation of the helical hairpin of domain 3, which contributes the other significant syntaxin 1a binding sites in the rat nSec1/syntaxin 1a complex structure but adopts multiple conformations in the unliganded s-Sec1 structures reported here. |
==About this Structure== | ==About this Structure== | ||
| - | 1FVF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Loligo_plei Loligo plei]. Full crystallographic information is available from [http:// | + | 1FVF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence 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=1FVF OCA]. |
==Reference== | ==Reference== | ||
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[[Category: parallel beta-sheets]] | [[Category: parallel beta-sheets]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:43:00 2008'' |
Revision as of 10:43, 21 February 2008
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CRYSTAL STRUCTURE ANALYSIS OF NEURONAL SEC1 FROM THE SQUID L. PEALEI
Overview
Sec1 molecules associate with t-SNAREs from the syntaxin family in a heterodimeric complex that plays an essential role in vesicle transport and membrane fusion. Neuronal rat n-Sec1 has an arch-shaped three-domain structure, which binds syntaxin 1a through contacts in domains 1 and 3. In both rat nSec1 and homologous squid s-Sec1, a potential effector-molecule binding-pocket is shaped by residues from domains 1 and 2 and is localized on the opposite side of the syntaxin 1a interaction site. Comparison of several crystal forms of unliganded neuronal squid Sec1 indicates a hinge region between domains 1 and 2 which allows domain 1 to rotate along a central axis. This movement could release syntaxin 1a upon interaction with a yet unspecified Sec1 effector molecule(s). The binding of an effector protein may also directly affect the conformation of the helical hairpin of domain 3, which contributes the other significant syntaxin 1a binding sites in the rat nSec1/syntaxin 1a complex structure but adopts multiple conformations in the unliganded s-Sec1 structures reported here.
About this Structure
1FVF is a Single protein structure of sequence from Loligo plei. Full crystallographic information is available from OCA.
Reference
Crystal structures of neuronal squid Sec1 implicate inter-domain hinge movement in the release of t-SNAREs., Bracher A, Weissenhorn W, J Mol Biol. 2001 Feb 9;306(1):7-13. PMID:11178889
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