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• W2125514891 abstract "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." @default.
• W2125514891 created "2016-06-24" @default.
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• W2125514891 date "2007-10-23" @default.
• W2125514891 modified "2023-09-27" @default.
• W2125514891 title "Structure of Human Synaptotagmin 1 C2AB in the Absence of Ca²⁺ Reveals a Novel Domain Association^," @default.
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• W2125514891 doi "https://doi.org/10.1021/bi701651k" @default.
• W2125514891 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5975968" @default.
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• W2125514891 hasPublicationYear "2007" @default.
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