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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

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 reverse transcriptase; HIV; nucleotide excision; AZTppppA; AZT resistance
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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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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