Structural highlights
Function
[SNP25_RAT] 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.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The structure of a truncated SNARE complex has been solved to 1.4-A resolution revealing a stabilizing salt bridge, sites of hydration, and conformational variability of the ionic central layer that were not observed in a previously published structure at 2.4-A resolution (Sutton, R. B., Fasshauer, D., Jahn, R., and Brunger, A. T. (1998) Nature 395, 347-353). The truncated complex lacks residues involved in phospholipid binding and denatures at a lower temperature than longer complexes as assessed by SDS and circular dichroism thermal melts. The truncated SNARE complex is monomeric, and it retains binding to synaptotagmin I.
High resolution structure, stability, and synaptotagmin binding of a truncated neuronal SNARE complex.,Ernst JA, Brunger AT J Biol Chem. 2003 Mar 7;278(10):8630-6. Epub 2002 Dec 20. PMID:12496247[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ernst JA, Brunger AT. High resolution structure, stability, and synaptotagmin binding of a truncated neuronal SNARE complex. J Biol Chem. 2003 Mar 7;278(10):8630-6. Epub 2002 Dec 20. PMID:12496247 doi:http://dx.doi.org/10.1074/jbc.M211889200
