| Structural highlights
2n1t is a 5 chain structure with sequence from Buffalo rat and Human. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Related: | 1sfc, 1uow |
| Gene: | Syb2, Vamp2 (Buffalo rat), Sap, Stx1a (Buffalo rat), SNAP, SNAP25, SNAP-25A (HUMAN), SVP65, SYT, SYT1 (HUMAN) |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[SNP25_HUMAN] t-SNARE involved in the molecular regulation of neurotransmitter release. May play an important role in the synaptic function of specific neuronal systems. Associates with proteins involved in vesicle docking and membrane fusion. Regulates plasma membrane recycling through its interaction with CENPF. [VAMP2_RAT] Involved in the targeting and/or fusion of transport vesicles to their target membrane (By similarity). [STX1A_RAT] Potentially involved in docking of synaptic vesicles at presynaptic active zones. May play a critical role in neurotransmitter exocytosis. May mediate Ca(2+)-regulation of exocytosis acrosomal reaction in sperm. [SYT1_HUMAN] May have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone. A Ca(2+)-dependent interaction between synaptotagmin and putative receptors for activated protein kinase C has also been reported. It can bind to at least three additional proteins in a Ca(2+)-independent manner; these are neurexins, syntaxin and AP2.
Publication Abstract from PubMed
Rapid neurotransmitter release depends on the Ca2+ sensor Synaptotagmin-1 (Syt1) and the SNARE complex formed by synaptobrevin, syntaxin-1 and SNAP-25. How Syt1 triggers release has been unclear, partly because elucidating high-resolution structures of Syt1-SNARE complexes has been challenging. An NMR approach based on lanthanide-induced pseudocontact shifts now reveals a dynamic binding mode in which basic residues in the concave side of the Syt1 C2B-domain beta-sandwich interact with a polyacidic region of the SNARE complex formed by syntaxin-1 and SNAP-25. The physiological relevance of this dynamic structural model is supported by mutations in basic residues of Syt1 that markedly impair SNARE-complex binding in vitro and Syt1 function in neurons. Mutations with milder effects on binding have correspondingly milder effects on Syt1 function. Our results support a model whereby dynamic interaction facilitates cooperation between Syt1 and the SNAREs in inducing membrane fusion.
Dynamic binding mode of a Synaptotagmin-1-SNARE complex in solution.,Brewer KD, Bacaj T, Cavalli A, Camilloni C, Swarbrick JD, Liu J, Zhou A, Zhou P, Barlow N, Xu J, Seven AB, Prinslow EA, Voleti R, Haussinger D, Bonvin AM, Tomchick DR, Vendruscolo M, Graham B, Sudhof TC, Rizo J Nat Struct Mol Biol. 2015 Jun 1. doi: 10.1038/nsmb.3035. PMID:26030874[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Brewer KD, Bacaj T, Cavalli A, Camilloni C, Swarbrick JD, Liu J, Zhou A, Zhou P, Barlow N, Xu J, Seven AB, Prinslow EA, Voleti R, Haussinger D, Bonvin AM, Tomchick DR, Vendruscolo M, Graham B, Sudhof TC, Rizo J. Dynamic binding mode of a Synaptotagmin-1-SNARE complex in solution. Nat Struct Mol Biol. 2015 Jun 1. doi: 10.1038/nsmb.3035. PMID:26030874 doi:http://dx.doi.org/10.1038/nsmb.3035
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