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1KIL

Three-dimensional structure of the complexin/SNARE complex

Summary for 1KIL
Entry DOI10.2210/pdb1kil/pdb
DescriptorSynaptobrevin SNARE motif, Syntaxin SNARE motif short, SNAP-25 N-terminal SNARE motif, ... (7 entities in total)
Functional Keywordshelix bound to four helix bundle, membrane protein
Biological sourceRattus norvegicus (Norway rat)
More
Cellular locationCytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Single-pass type IV membrane protein: P63045
Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Single-pass type IV membrane protein (By similarity): P32851
Cytoplasm, perinuclear region (By similarity): P60880 P60880
Cytoplasm, cytosol: P63041
Total number of polymer chains5
Total formula weight36923.73
Authors
Chen, X.,Tomchick, D.,Kovrigin, E.,Arac, D.,Machius, M.,Sudhof, T.C.,Rizo, J. (deposition date: 2001-12-03, release date: 2002-03-13, Last modification date: 2023-08-16)
Primary citationChen, X.,Tomchick, D.R.,Kovrigin, E.,Arac, D.,Machius, M.,Sudhof, T.C.,Rizo, J.
Three-dimensional structure of the complexin/SNARE complex.
Neuron, 33:397-409, 2002
Cited by
PubMed Abstract: During neurotransmitter release, the neuronal SNARE proteins synaptobrevin/VAMP, syntaxin, and SNAP-25 form a four-helix bundle, the SNARE complex, that pulls the synaptic vesicle and plasma membranes together possibly causing membrane fusion. Complexin binds tightly to the SNARE complex and is essential for efficient Ca(2+)-evoked neurotransmitter release. A combined X-ray and TROSY-based NMR study now reveals the atomic structure of the complexin/SNARE complex. Complexin binds in an antiparallel alpha-helical conformation to the groove between the synaptobrevin and syntaxin helices. This interaction stabilizes the interface between these two helices, which bears the repulsive forces between the apposed membranes. These results suggest that complexin stabilizes the fully assembled SNARE complex as a key step that enables the exquisitely high speed of Ca(2+)-evoked neurotransmitter release.
PubMed: 11832227
DOI: 10.1016/S0896-6273(02)00583-4
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.3 Å)
Structure validation

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건을2024-11-06부터공개중

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