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LRP6 structure. (A) Schematic representation of human LRP6 domains: βp, YWTD β-propeller domains; CD, cytoplasmic domain; E, EGF-like domains; L, LDLR type A repeats; S, signal peptide; TM, transmembrane domain. The five PPP(S/T)P phosphorylation motifs are shown in red. (B) LRP6 ectodomain in its resting state. In absence of ligands, LRP6 undergoes a large bending/unbending motion, preventing homodimer and signalosome formation [14].
