Fig. 1: Structure of the inactive FZD7 dimer mediated by a lipidic interface. | Nature Communications

Fig. 1: Structure of the inactive FZD7 dimer mediated by a lipidic interface.

From: Structural basis of frizzled 7 activation and allosteric regulation

Fig. 1

a Cryo-EM density map of the FZD7 dimer with C2 symmetry, colored by monomer, with an intermolecular layer of lipids sandwiched between the monomers, shown in red. b Atomic arrangement of the FZD7 dimer shown with a close-up side view of the compact interface presenting with endogenous 1-palmitoyl-2-oleoyl-phosphatidylcholine (POPC) and two major cholesterol hemisuccinate (CHS) molecules, which altogether mediate and stabilize the interface between the monomers. c Overall organization of the extracellular region of FZD7 with ECL1, ECL2, ECL3, and the hinge region which altogether form a peripheral lid over the transmembrane bundle. d A top view of the helical bundle depicts the folded β-stranded structure of ECL2 with K5337.41 and Y5347.42 rendering blockage of the receptor core. e Map of the surface electrostatic potential of the internal cavity highlighting the bottleneck in modulating entry of water molecules.

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