 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 3]](nw5029fig3mag.jpg)
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Figure 3
Comparison of the dNTP-binding sites. (a) Multiple sequence alignment of HIV-1 RT, human HBV Pol RT domain and Duck hepatitis B virus (DHBV) Pol RT domain. Secondary structures of HIV-1 RT are indicated at the top (α, α-helix; β, β-strand; η, 310-helix). The Q151M mutational point is indicated by a red arrow. Residues forming the dNTP-binding site are denoted by black stars. The conserved motifs among the various types of RTs are indicated by black boxes. Each protein sequence was aligned by ClustalW (Larkin et al., 2007  ) and the figure was prepared with ESPript (Robert & Gouet, 2014). (b), (c) and (d) show the dNTP-binding pockets of HIV-1 RT Q151M, HIV-1 RT with bound DNA and azidothymidine triphosphate (AZT; PDB entry 3v4i
) and HIV-1 RT with bound DNA and tenofovir diphosphate (TNV; PDB entry 1t05
), respectively. Residues that form the dNTP-binding site are displayed as stick models. The final 2mFo − DFc map of Met151 is shown in blue contoured at the 1.0σ level. DNA molecules are shown as white ribbon models. AZT and TNV are coloured black and shown as ball-and-stick models. Green spheres indicate Mg2+ ions coordinated to the phosphate groups of the inhibitors and Asp110 and Asp185. Dashed lines indicate hydrogen bonds in the dNTP-binding pocket. |
![[Figure 3]](nw5029fig3.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
