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

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; in revised form: 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

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MDPI and ACS Style

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.

AMA Style

Scott WA. Structures of Reverse Transcriptase Pre- and Post-Excision Complexes Shed New Light on HIV-1 AZT Resistance. Viruses. 2011; 3(1):20-25.

Chicago/Turabian Style

Scott, Walter A. 2011. "Structures of Reverse Transcriptase Pre- and Post-Excision Complexes Shed New Light on HIV-1 AZT Resistance." Viruses 3, no. 1: 20-25.

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