1dn1: Difference between revisions

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[[Image:1dn1.jpg|left|200px]]<br /><applet load="1dn1" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1dn1.jpg|left|200px]]<br /><applet load="1dn1" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1dn1, resolution 2.60Å" />

'''CRYSTAL STRUCTURE OF THE NEURONAL-SEC1/SYNTAXIN 1A COMPLEX'''<br />

==Overview==

Syntaxin 1a and neuronal Sec1 (nSec1) form an evolutionarily conserved, heterodimer that is essential for vesicle trafficking and membrane fusion., The crystal structure of the nSec1-syntaxin 1a complex, determined at 2.6, A resolution, reveals that major conformational rearrangements occur in, syntaxin relative to both the core SNARE complex and isolated syntaxin. We, identify regions of the two proteins that seem to determine the binding, specificity of particular Sec1 proteins for syntaxin isoforms, which is, likely to be important for the fidelity of membrane trafficking. The, structure also indicates mechanisms that might couple the action of, upstream effector proteins to conformational changes in syntaxin 1a and, nSec1 that lead to core complex formation and membrane fusion.

Syntaxin 1a and neuronal Sec1 (nSec1) form an evolutionarily conserved heterodimer that is essential for vesicle trafficking and membrane fusion. The crystal structure of the nSec1-syntaxin 1a complex, determined at 2.6 A resolution, reveals that major conformational rearrangements occur in syntaxin relative to both the core SNARE complex and isolated syntaxin. We identify regions of the two proteins that seem to determine the binding specificity of particular Sec1 proteins for syntaxin isoforms, which is likely to be important for the fidelity of membrane trafficking. The structure also indicates mechanisms that might couple the action of upstream effector proteins to conformational changes in syntaxin 1a and nSec1 that lead to core complex formation and membrane fusion.

==About this Structure==

1DN1 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences 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=1DN1 OCA].

1DN1 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences 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=1DN1 OCA].

==Reference==

Line 13:

[[Category: Protein complex]]

[[Category: Rattus norvegicus]]

[[Category: Misura, K.M.S.]]

[[Category: Misura, K M.S.]]

[[Category: Scheller, R.H.]]

[[Category: Scheller, R H.]]

[[Category: Weis, W.I.]]

[[Category: Weis, W I.]]

[[Category: multi-subunit]]

[[Category: protein-protein complex]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20 13~~:25:~~32 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:18:19 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1dn1.jpg|left|200px]]<br /><applet load="1dn1" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1dn1.jpg|left|200px]]<br /><applet load="1dn1" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1dn1, resolution 2.60&Aring;" />
 '''CRYSTAL STRUCTURE OF THE NEURONAL-SEC1/SYNTAXIN 1A COMPLEX'''<br />
 ==Overview==
-Syntaxin 1a and neuronal Sec1 (nSec1) form an evolutionarily conserved, heterodimer that is essential for vesicle trafficking and membrane fusion., The crystal structure of the nSec1-syntaxin 1a complex, determined at 2.6, A resolution, reveals that major conformational rearrangements occur in, syntaxin relative to both the core SNARE complex and isolated syntaxin. We, identify regions of the two proteins that seem to determine the binding, specificity of particular Sec1 proteins for syntaxin isoforms, which is, likely to be important for the fidelity of membrane trafficking. The, structure also indicates mechanisms that might couple the action of, upstream effector proteins to conformational changes in syntaxin 1a and, nSec1 that lead to core complex formation and membrane fusion.
+Syntaxin 1a and neuronal Sec1 (nSec1) form an evolutionarily conserved heterodimer that is essential for vesicle trafficking and membrane fusion. The crystal structure of the nSec1-syntaxin 1a complex, determined at 2.6 A resolution, reveals that major conformational rearrangements occur in syntaxin relative to both the core SNARE complex and isolated syntaxin. We identify regions of the two proteins that seem to determine the binding specificity of particular Sec1 proteins for syntaxin isoforms, which is likely to be important for the fidelity of membrane trafficking. The structure also indicates mechanisms that might couple the action of upstream effector proteins to conformational changes in syntaxin 1a and nSec1 that lead to core complex formation and membrane fusion.
 ==About this Structure==
-DN1 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences 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=1DN1 OCA].
+DN1 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences 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=1DN1 OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Protein complex]]
 [[Category: Rattus norvegicus]]
-[[Category: Misura, K.M.S.]]
+[[Category: Misura, K M.S.]]
-[[Category: Scheller, R.H.]]
+[[Category: Scheller, R H.]]
-[[Category: Weis, W.I.]]
+[[Category: Weis, W I.]]
 [[Category: multi-subunit]]
 [[Category: protein-protein complex]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:25:32 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:18:19 2008''