Full-length [Gα.sub.q]-phospholipase C-β3 structure reveals interfaces of the C-terminal coiled-coil...
Full-length [Gα.sub.q]-phospholipase C-β3 structure reveals interfaces of the C-terminal coiled-coil domain
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Nature Publishing Group
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English
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Nature Publishing Group
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Phospholipase C-β (PLCβ) is directly activated by [Gα.sub.q], 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 [Gα.sub.q]. The distal CTD...
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Full title
Full-length [Gα.sub.q]-phospholipase C-β3 structure reveals interfaces of the C-terminal coiled-coil domain
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TN_cdi_gale_infotracmisc_A322026630
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https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_gale_infotracmisc_A322026630
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ISSN
1545-9993
DOI
10.1038/nsmb.2497
