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3RK2

Truncated SNARE complex

Summary for 3RK2
Entry DOI10.2210/pdb3rk2/pdb
Related3RK3
DescriptorVesicle-associated membrane protein 2, Syntaxin-1A, Synaptosomal-associated protein 25, ... (6 entities in total)
Functional Keywordssnare proteins, membrane fusion, membrane protein-exocytosis complex, membrane protein/exocytosis
Biological sourceHomo sapiens (human)
More
Cellular locationCytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Single-pass type IV membrane protein: P63027
Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Single-pass type IV membrane protein (By similarity): P32851
Cytoplasm, perinuclear region (By similarity): P60880 P60880
Total number of polymer chains8
Total formula weight57628.70
Authors
Kuemmel, D.,Reinisch, K.M. (deposition date: 2011-04-17, release date: 2011-07-27, Last modification date: 2023-09-13)
Primary citationKummel, D.,Krishnakumar, S.S.,Radoff, D.T.,Li, F.,Giraudo, C.G.,Pincet, F.,Rothman, J.E.,Reinisch, K.M.
Complexin cross-links prefusion SNAREs into a zigzag array.
Nat.Struct.Mol.Biol., 18:927-933, 2011
Cited by
PubMed Abstract: Complexin prevents SNAREs from releasing neurotransmitters until an action potential arrives at the synapse. To understand the mechanism for this inhibition, we determined the structure of complexin bound to a mimetic of a prefusion SNAREpin lacking the portion of the v-SNARE that zippers last to trigger fusion. The 'central helix' of complexin is anchored to one SNARE complex, while its 'accessory helix' extends away at ~45° and bridges to a second complex, occupying the vacant v-SNARE binding site to inhibit fusion. We expected the accessory helix to compete with the v-SNARE for t-SNARE binding but found instead that the interaction occurs intermolecularly. Thus, complexin organizes the SNAREs into a zigzag topology that, when interposed between the vesicle and plasma membranes, is incompatible with fusion.
PubMed: 21785414
DOI: 10.1038/nsmb.2101
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.2 Å)
Structure validation

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