Figure 6: Comparison between the crystal structures of WT-TTR, TTR A108V and TTR A108I. | Scientific Reports

Figure 6: Comparison between the crystal structures of WT-TTR, TTR A108V and TTR A108I.

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

Figure 6

(A) Superposition of TTR WT (pink), A108V (blue) and A108I (green) tetramers show overall rmsd for the superposed Cα atoms are 0.40 Å and 0.38 Å, respectively. (B) Rotation about y-axis makes possible to see that side-chain of residues at position 108 (gray-scale sticks) extend more and more inside of T4 channels in order Ala, Val and Ile108 variants.

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