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Function
Synapsins (SYN) are neuronal phosphoproteins which modulate neurotransmitter release at the pre-synaptic terminal by reversibly tethering synaptic vescicles to the actin cytoskeleton[1].
Structural highlights
The 3D structure of the rat synapsin 1 complex with ATP shows the catalytically essential multifunctional loop surrounding the ATP which makes both hydrogen bonds and Van-der Waals contacts with the protein[2]. Water molecules are shown as red spheres.
- ↑ Cesca F, Baldelli P, Valtorta F, Benfenati F. The synapsins: key actors of synapse function and plasticity. Prog Neurobiol. 2010 Aug;91(4):313-48. doi: 10.1016/j.pneurobio.2010.04.006. Epub, 2010 May 10. PMID:20438797 doi:https://dx.doi.org/10.1016/j.pneurobio.2010.04.006
- ↑ Brautigam CA, Chelliah Y, Deisenhofer J. Tetramerization and ATP binding by a protein comprising the A, B, and C domains of rat synapsin I. J Biol Chem. 2004 Mar 19;279(12):11948-56. Epub 2003 Dec 19. PMID:14688264 doi:10.1074/jbc.M312015200
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3D structures of synapsin
Updated on 15-August-2024
{"openlevels":0}
- Synapsin 1
- 1auv - bSYN1A C-terminal 110-421 - bovine
- 1aux - bSYN1A C-terminal + ATPgS
- 1pk8, 1px2 - rSYN1 + ATP - rat
- Synapsin 2
- 1i7n - rSYN2 C-terminal
- 1i7l - rSYN2 C-terminal + ATP
- Synapsin 3
- 2p0a - hSYN3 actin-binding+synaptic vescicle binding domains 76-417 + AMPPNP - human
References
