2r83
Crystal structure analysis of human synaptotagmin 1 C2A-C2B
| |||||||
| , resolution 2.70Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , , , , , and | ||||||
| Ligands: | |||||||
| Gene: | SYT1, SVP65, SYT (Homo sapiens) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
OverviewOverview
Release of neurotransmitter from synaptic vesicles requires the Ca2+/phospholipid-binding protein synaptotagmin 1. There is considerable evidence that cooperation between the tandem C2 domains of synaptotagmin is a requirement of regulated exocytosis; however, high-resolution structural evidence for this interaction has been lacking. The 2.7 A crystal structure of the cytosolic domains of human synaptotagmin 1 in the absence of Ca2+ reveals a novel closed conformation of the protein. The shared interface between C2A and C2B is stabilized by a network of interactions between residues on the C-terminal alpha-helix of the C2B domain and residues on loops 1-3 of the Ca2+-binding region of C2A. These interactions alter the overall shape of the Ca2+-binding pocket of C2A, but not that of C2B. Thus, synaptotagmin 1 C2A-C2B may utilize a novel regulatory mechanism whereby one C2 domain could regulate the other until an appropriate triggering event decouples them.
About this StructureAbout this Structure
2R83 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Structure of human synaptotagmin 1 C2AB in the absence of Ca2+ reveals a novel domain association., Fuson KL, Montes M, Robert JJ, Sutton RB, Biochemistry. 2007 Nov 13;46(45):13041-8. Epub 2007 Oct 23. PMID:17956130
Page seeded by OCA on Thu Mar 20 18:33:26 2008