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Viruses 2011, 3(1), 20-25; doi:10.3390/v3010020

Structures of Reverse Transcriptase Pre- and Post-Excision Complexes Shed New Light on HIV-1 AZT Resistance

Department of Biochemistry and Molecular Biology, University of Miami Miller School of Medicine, P.O. Box 016129, Miami, FL 33101, USA
Received: 31 December 2010 / Revised: 13 January 2011 / Accepted: 13 January 2011 / Published: 18 January 2011
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Abstract

HIV-1 resistance to 3'-azido-2',3'-deoxythymidine (AZT, zidovudine) results from mutations in reverse transcriptase that increase the ability of the enzyme to excise AZT-monophosphate after it has been incorporated. Crystal structures of complexes of wild type and mutant reverse transcriptase with double-stranded DNA with or without the excision product, AZT adenosine dinucleoside tetraphosphate (AZTppppA), have recently been reported [1]. The excision-enhancing mutations dramatically change the way the enzyme interacts with the excision product.
Keywords: reverse transcriptase; HIV; nucleotide excision; AZTppppA; AZT resistance reverse transcriptase; HIV; nucleotide excision; AZTppppA; AZT resistance
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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Scott, W.A. Structures of Reverse Transcriptase Pre- and Post-Excision Complexes Shed New Light on HIV-1 AZT Resistance. Viruses 2011, 3, 20-25.

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