Figure 7: Tetrameric interfaces of the TTR WT and, A108V and A108I variants. | Scientific Reports

Figure 7: Tetrameric interfaces of the TTR WT and, A108V and A108I variants.

From: Cavity filling mutations at the thyroxine-binding site dramatically increase transthyretin stability and prevent its aggregation

Figure 7

(A) Cartoon diagrams of the TTR homotetramers showing the spatial orientation of residue A/V/I108 (black spheres) inside of the ligand binding pockets. (B) A glimpse in the thyroxine binding channel showing the new interactions formed after mutations that strengthen the dimer-dimer packing of these variants. Side-chains of the residues Leu17, Ala/Val/Leu108, Leu110, Thr119, Val121, important for protein stability, are shown in stick representation. The electron density maps are contoured at 1.5σ. Images were drawn with PyMOL.

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