1dn1
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CRYSTAL STRUCTURE OF THE NEURONAL-SEC1/SYNTAXIN 1A COMPLEX
OverviewOverview
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 StructureAbout this Structure
1DN1 is a Protein complex structure of sequences from Rattus norvegicus. Full crystallographic information is available from OCA.
ReferenceReference
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:10746715
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