HIV-1 Reverse Transcriptase Structure with RNase H Inhibitor Dihydroxy Benzoyl Naphthyl Hydrazone Bound at a Novel Site

The rapid emergence of drug-resistant variants of human immunodeficiency virus, type 1 (HIV-1), has limited the efficacy of anti-acquired immune deficiency syndrome (AIDS) treatments, and new lead compounds that target novel binding sites are needed. We have determined the 3.15 Å resolution crystal...

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Veröffentlicht in:	ACS chemical biology 2006-12, Vol.1 (11), p.702-712
Hauptverfasser:	Himmel, Daniel M, Sarafianos, Stefan G, Dharmasena, Sanjeewa, Hossain, Mohammed M, McCoy-Simandle, Kessler, Ilina, Tatiana, Clark, Arthur D, Knight, Jennifer L, Julias, John G, Clark, Patrick K, Krogh-Jespersen, Karsten, Levy, Ronald M, Hughes, Stephen H, Parniak, Michael A, Arnold, Eddy
Format:	Artikel
Sprache:	eng
Schlagworte:	Cell Line, Tumor HIV Reverse Transcriptase - antagonists & inhibitors HIV Reverse Transcriptase - chemistry HIV Reverse Transcriptase - metabolism Humans Hydrazones - chemistry Hydrazones - pharmacology Protein Binding - drug effects Protein Binding - physiology Protein Structure, Secondary - drug effects Protein Structure, Secondary - physiology Reverse Transcriptase Inhibitors - chemistry Reverse Transcriptase Inhibitors - pharmacology Ribonuclease H - antagonists & inhibitors Ribonuclease H - metabolism Structure-Activity Relationship
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