Figure 3: Crystal structures of WT-TTR/ligand and V122I-TTR/ligand complexes. | Nature Communications

Figure 3: Crystal structures of WT-TTR/ligand and V122I-TTR/ligand complexes.

From: Repositioning tolcapone as a potent inhibitor of transthyretin amyloidogenesis and associated cellular toxicity

Figure 3

(a) Global view of WT-TTR bound to tolcapone (ribbon representation). The electron density map of the two T4-binding sites of tolcapone are depicted. Broken line indicates the twofold symmetry axis of the dimer–dimer interface. Detailed and close up view of one of the WT-TTR T4-binding sites are shown in b for tolcapone (PDB: 4D7B) and c for tafamidis (PDB: 3TCT). (d) Global view of V122I-TTR bound to tolcapone (ribbon representation). The electron density map of the two T4-binding sites of tolcapone are depicted. Broken line indicates the twofold symmetry axis of the dimer–dimer interface. Detailed and close up view of one of the V122I-TTR T4-binding sites are shown in e for tolcapone (PDB: 5A6I), and f for tafamidis (PDB: 4HIS). Ligands and some of the TTR interacting residues are represented by sticks. Electron densities of the two structures are shown in Supplementary Fig. 5.

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