Fig. 1: Cryo-EM structure of an antagonized aPKCι–Par6α–Llgl1 polarity complex. | Nature Structural & Molecular Biology

Fig. 1: Cryo-EM structure of an antagonized aPKCι–Par6α–Llgl1 polarity complex.

From: Capture, mutual inhibition and release mechanism for aPKC–Par6 and its multisite polarity substrate Lgl

Fig. 1: Cryo-EM structure of an antagonized aPKCι–Par6α–Llgl1 polarity complex.

a, Surface rendering of the aPKCι–Par6α–Llgl1 cryo-EM structure. Surfaces for individual components are colored differently: Par6, salmon; aPKCι, yellow; Llgl1, light blue; Llgl1 loop (10–11) containing the P-site, navy. b, Ribbon diagram of the aPKCι–Par6α–Llgl1 complex, colored as in a. A stick representation for AMP-PNP is shown indicating the aPKCι nucleotide-binding site and the three phospho-residues aPKCιpT412, aPKCιpT564 and Llgl1pS663. c, Schematic of key interactions mapped onto the domain structures for each component. Grayed out segments indicate regions not defined in the final model. d, Schematized aPKCι–Par6α–Llgl1 structure showing two orthogonal slices through the structure with a similar view to b, mapping the approximate location of crucial interaction contacts and phospho-acceptor serine residues. e, Alignment of loop (10–11) sequences for Lgl homologs indicating conservation at opposing ends of the membrane-binding loop. The Lgl P-site and PBM are indicated. Phospho-acceptor sites and interaction contacts are colored as in c.

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