1jth
From Proteopedia
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Crystal structure and biophysical properties of a complex between the N-terminal region of SNAP25 and the SNARE region of syntaxin 1a
Overview
SNARE proteins are required for intracellular membrane fusion. In the, neuron, the plasma membrane SNAREs syntaxin 1a and SNAP25 bind to VAMP2, found on neurotransmitter-containing vesicles. These three proteins, contain "SNARE regions" that mediate their association into stable, tetrameric coiled-coil structures. Syntaxin 1a contributes one such, region, designated H3, and SNAP25 contributes two SNARE regions to the, fusogenic complex with VAMP2. Syntaxin 1a H3 (syn1aH3) and SNAP25 can form, a stable assembly, which can then be bound by VAMP2 to form the full SNARE, complex. Here we show that syn1aH3 can also form a stable but kinetically, trapped complex with the N-terminal SNARE region of SNAP25 (S25N). The, crystal structure of this complex reveals an extended parallel four-helix, bundle similar to that of the core SNARE and the syn1aH3-SNAP25 complexes., The inherent ability of syn1aH3 and S25N to associate stably in vitro, implies that the intracellular fusion machinery must prevent formation of, or remove, any non-productive complexes. Comparison with the, syn1aH3-SNAP25 complex suggests that the linkage of the N- and C-terminal, SNAP25 SNARE regions is kinetically advantageous in preventing formation, of the non-productive syn1aH3-S25N complex. We also demonstrate that the, syn1aH3-S25N complex can be disassembled by alpha-SNAP and, N-ethylmaleimide-sensitive factor.
About this Structure
1JTH is a Protein complex structure of sequences from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Crystal structure and biophysical properties of a complex between the N-terminal SNARE region of SNAP25 and syntaxin 1a., Misura KM, Gonzalez LC Jr, May AP, Scheller RH, Weis WI, J Biol Chem. 2001 Nov 2;276(44):41301-9. Epub 2001 Aug 30. PMID:11533035
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