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| [[Image:1dn1.jpg|left|200px]]<br /><applet load="1dn1" size="350" color="white" frame="true" align="right" spinBox="true" | | #REDIRECT [[3c98]] This PDB entry is obsolete and replaced by 3c98 |
| caption="1dn1, resolution 2.60Å" />
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| '''CRYSTAL STRUCTURE OF THE NEURONAL-SEC1/SYNTAXIN 1A COMPLEX'''<br />
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| ==Overview==
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| 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.
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| ==About this Structure==
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| 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].
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| ==Reference==
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| Three-dimensional structure of the neuronal-Sec1-syntaxin 1a complex., Misura KM, Scheller RH, Weis WI, Nature. 2000 Mar 23;404(6776):355-62. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10746715 10746715]
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| [[Category: Protein complex]]
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| [[Category: Rattus norvegicus]]
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| [[Category: Misura, K M.S.]]
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| [[Category: Scheller, R H.]]
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| [[Category: Weis, W I.]]
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| [[Category: multi-subunit]]
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| [[Category: protein-protein complex]]
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| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:18:19 2008''
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This PDB entry is obsolete and replaced by 3c98