Dynamic structure of lipid-bound synaptobrevin suggests a nucleation-propagation mechanism for trans...
Dynamic structure of lipid-bound synaptobrevin suggests a nucleation-propagation mechanism for trans-SNARE complex formation
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United States: National Academy of Sciences
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English
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United States: National Academy of Sciences
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The synaptic vesicle protein synaptobrevin engages with syntaxin and SNAP-25 to form the SNARE complex, which drives membrane fusion in neuronal exocytosis. In the SNARE complex, the SNARE motif of synaptobrevin forms a 55-residue helix, but it has been assumed to be mostly unstructured in its prefusion form. NMR data for full-length synaptobrevin...
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Dynamic structure of lipid-bound synaptobrevin suggests a nucleation-propagation mechanism for trans-SNARE complex formation
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TN_cdi_pnas_primary_106_48_20306
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https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pnas_primary_106_48_20306
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0027-8424
E-ISSN
1091-6490
DOI
10.1073/pnas.0908317106