Fig. 3: Structural consequences of humanizing residues in OWM and NWM NTCP.
From: Targeted viral adaptation generates a simian-tropic hepatitis B virus that infects marmoset cells

A Molecular surface model showing the hNTCP functional tunnel (PDB: 7PQQ) and the TM5 region in different NTCP orthologues. B Structure alignment of the TM4-5 region of hNTCP (PDB: 7PQG), OWMWT, OWMR158G and OWMR158G, P165L. A helix in the TM4-5 loop in hNTCP and OWMR158G, P165L can increase NTCP stability. C NTCP structures with side chains in residue 84–87 for hNTCP (PDB: 7PQG), marmoset, squirrel monkey (SqM) and their variants. The hydropathicity and instability index indicating the biophysical properties of residues 84–87 were calculated in Protein 3D (DNASTAR Inc., Madison, WI). D Structure alignment of different NTCPs (hNTCP structure from PDB: 7PQG). Similarity assay conducted by root mean squared deviation (RMSD). OWM old world monkey, SqM squirrel monkey, WT wild type, Cyno cynomolgus machaca, TM transmembrane.