HIV-1 Reverse Transcriptase Still Remains a New Drug Target: Structure, Function, Classical Inhibitors, and New Inhibitors with Innovative Mechanisms of Actions
Figure 2
Structure of HIV-1 RT. The enzyme has two domains: the p66 (colored) and the p51 (gray). The polymerase domain shows a characteristic highly conserved structure that resembles a right hand, consisting of fingers domain (magenta), palm domain (cyan), thumb domain (blue). The p66 subunit also comprises the connection domain (orange) and RNase H domain (yellow). The polymerase active site is located in the middle of palm, fingers, and thumb subdomains. The three catalytic aspartic acid residues (D110, D185 and D186) located in the palm subdomain of p66 that bind the cofactor divalent ions () are shown (red). The RNase H domain is located at C-terminus of the p66 subunit, 60 Å far from polymerase active site. The RNase H active site contains a DDE motif comprising the carboxylates residues D443, E478, D498, and D549 that can coordinate two divalent .
