Fig. 2: Structural comparison of conserved motifs in the inactive and active FZD7 conformations. | Nature Communications

Fig. 2: Structural comparison of conserved motifs in the inactive and active FZD7 conformations.

From: Structural basis of frizzled 7 activation and allosteric regulation

Fig. 2

The intracellular rearrangements of conserved residue a P4816.43, b extended molecular switch residues, F4746.36 - W5476.36, e Y4786.40 and f molecular switch residues W5477.55 - R4706.32 are observed upon agonist binding. c A network of extended polar contacts in ICL3 is made between the two conformations of FZD7. d Comparison of the nucleotide-free Gαs-bound FZD7 (pink, PDB: 7EVW) and inactive FZD7 (purple) highlighting structural changes of conserved residues and regions of interest. g G protein binding rearranges residues in ICL1 involving D2781.57, F282, R281, R280, and M279. Scatterplot of occurring χ1 χ2 dihedral angles of residue h W3543.43 and i W5477.55 calculated for each frame (50 ps time steps) over the trajectory from replica 1 of FZD7 simulations of active and inactive state.

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