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• W2080854025 abstract "The regulatory importance of the C-terminal coiled-coil domain of PLCβ has long been known yet remains poorly understood. The crystal structure and cryo-EM reconstruction of full-length PLCβ3 bound to its activator Gαq reveals that the C terminus makes contact with both the catalytic core and Gαq to contribute to the complex regulation of the enzyme. Phospholipase C-β (PLCβ) is directly activated by Gαq, but the molecular basis for how its distal C-terminal domain (CTD) contributes to maximal activity is poorly understood. Herein we present both the crystal structure and cryo-EM three-dimensional reconstructions of human full-length PLCβ3 in complex with mouse Gαq. The distal CTD forms an extended monomeric helical bundle consisting of three antiparallel segments with structural similarity to membrane-binding bin-amphiphysin-Rvs (BAR) domains. Sequence conservation of the distal CTD suggests putative membrane and protein interaction sites, the latter of which bind the N-terminal helix of Gαq in both the crystal structure and cryo-EM reconstructions. Functional analysis suggests that the distal CTD has roles in membrane targeting and in optimizing the orientation of the catalytic core at the membrane for maximal rates of lipid hydrolysis." @default.
• W2080854025 created "2016-06-24" @default.
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• W2080854025 date "2013-02-03" @default.
• W2080854025 modified "2023-10-18" @default.
• W2080854025 title "Full-length Gαq–phospholipase C-β3 structure reveals interfaces of the C-terminal coiled-coil domain" @default.
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• W2080854025 doi "https://doi.org/10.1038/nsmb.2497" @default.
• W2080854025 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3594540" @default.
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