Extended Data Fig. 3: cryo-EM map of structural elements of palmitoleoyl-CoA-bound and LGK974-bound PORCN.
From: Mechanisms and inhibition of Porcupine-mediated Wnt acylation
a, The Fourier shell correlation (FSC) curves calculated between the refined structure model and the half map used for refinement (yellow), the other half map (gray) and the full map (blue) of palmitoleoyl-CoA-bound PORCN. b, Density map colored by local resolution estimation using cryoSPARC. c, The major helices of PORCN. d, MD simulation suggests that palmitoleoyl-CoA binds to PORCN in the curled-up conformation. After 100 ns simulations, the interaction between residues W300, H357 and the curled-down palmitoleoyl-CoA disrupts (the right bottom panel). The palmitoleoyl-CoA in either conformation with the cryo-EM map is shown. e, The Fourier shell correlation (FSC) curves calculated between the refined structure model and the half map used for refinement (yellow), the other half map (gray) and the full map (blue) of palmitoleoylated WNT3A-bound PORCN. f, Density map colored by local resolution estimation using cryoSPARC. g, The major helices of PORCN.
