Two‐metal ion mechanism of RNA cleavage by HIV RNase H and mechanism‐based design of selective HIV RNase H inhibitors

Human immunodeficiency virus (HIV) RNase H activity is essential for the synthesis of viral DNA by HIV reverse transcriptase (HIV‐RT). RNA cleavage by RNase H requires the presence of divalent metal ions, but the role of metal ions in the mechanism of RNA cleavage has not been resolved. We measured...

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Veröffentlicht in:	Nucleic acids research 2003-12, Vol.31 (23), p.6852-6859
Hauptverfasser:	Klumpp, Klaus, Hang, Julie Qi, Rajendran, Surendran, Yang, Yanli, Derosier, Andre, Wong Kai In, Philippe, Overton, Hilary, Parkes, Kevin E. B., Cammack, Nick, Martin, Joseph A.
Format:	Artikel
Sprache:	eng
Schlagworte:	Binding Sites Cations, Divalent - metabolism Cations, Divalent - pharmacology Drug Design Enzyme Activation - drug effects Enzyme Inhibitors - pharmacology Escherichia coli - enzymology HIV - enzymology Human immunodeficiency virus Metals - metabolism Metals - pharmacology ribonuclease Ribonuclease H - antagonists & inhibitors Ribonuclease H - metabolism Substrate Specificity
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