Structural highlights
Function
[SYN1_RAT] Neuronal phosphoprotein that coats synaptic vesicles, binds to the cytoskeleton, and is believed to function in the regulation of neurotransmitter release.
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
Synapsins are multidomain proteins that are critical for regulating neurotransmitter release in vertebrates. In the present study, two crystal structures of the C domain of rat synapsin I (rSynI-C) in complex with Ca(2+) and ATP reveal that this protein can form a tetramer and that a flexible loop (the "multifunctional loop") contacts bound ATP. Further experiments were carried out on a protein comprising the A, B, and C domains of rat synapsin I (rSynI-ABC). An ATP-stabilized tetramer of rSynI-ABC is observed during velocity sedimentation and size-exclusion chromatographic experiments. These hydrodynamic results also indicate that the A and B domains exist in an extended conformation. Calorimetric measurements of ATP binding to wild-type and mutant rSynI-ABC demonstrate that the multifunctional loop and a cross-tetramer contact are important for ATP binding. The evidence supports a view of synapsin I as an ATP-utilizing, tetrameric protein made up of monomers that have a flexible, extended N terminus.
Tetramerization and ATP binding by a protein comprising the A, B, and C domains of rat synapsin I.,Brautigam CA, Chelliah Y, Deisenhofer J J Biol Chem. 2004 Mar 19;279(12):11948-56. Epub 2003 Dec 19. PMID:14688264[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ 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
