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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...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pnas_primary_106_48_20306

Dynamic structure of lipid-bound synaptobrevin suggests a nucleation-propagation mechanism for trans-SNARE complex formation

About this item

Full title

Dynamic structure of lipid-bound synaptobrevin suggests a nucleation-propagation mechanism for trans-SNARE complex formation

Publisher

United States: National Academy of Sciences

Journal title

Proceedings of the National Academy of Sciences - PNAS, 2009-12, Vol.106 (48), p.20306-20311

Language

English

Formats

Publication information

Publisher

United States: National Academy of Sciences

More information

Scope and Contents

Contents

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...

Alternative Titles

Full title

Dynamic structure of lipid-bound synaptobrevin suggests a nucleation-propagation mechanism for trans-SNARE complex formation

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pnas_primary_106_48_20306

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pnas_primary_106_48_20306

Other Identifiers

ISSN

0027-8424

E-ISSN

1091-6490

DOI

10.1073/pnas.0908317106

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