Structure of HIV-1 Reverse Transcriptase with the Inhibitor β-Thujaplicinol Bound at the RNase H Active Site

Novel inhibitors are needed to counteract the rapid emergence of drug-resistant HIV variants. HIV-1 reverse transcriptase (RT) has both DNA polymerase and RNase H (RNH) enzymatic activities, but approved drugs that inhibit RT target the polymerase. Inhibitors that act against new targets, such as RN...

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Veröffentlicht in:	Structure (London) 2009-12, Vol.17 (12), p.1625-1635
Hauptverfasser:	Himmel, Daniel M., Maegley, Karen A., Pauly, Tom A., Bauman, Joseph D., Das, Kalyan, Dharia, Chhaya, Clark, Arthur D., Ryan, Kevin, Hickey, Michael J., Love, Robert A., Hughes, Stephen H., Bergqvist, Simon, Arnold, Eddy
Format:	Artikel
Sprache:	eng
Schlagworte:	Catalytic Domain Crystallography, X-Ray HIV Reverse Transcriptase - chemistry HIV Reverse Transcriptase - metabolism MICROBIO Models, Molecular Protein Binding Protein Conformation PROTEINS Reverse Transcriptase Inhibitors - chemistry Reverse Transcriptase Inhibitors - metabolism Ribonucleases - metabolism RNA Tropolone - analogs & derivatives Tropolone - chemistry Tropolone - metabolism
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