Structural basis of HIV-1 resistance to AZT by excision

  title={Structural basis of HIV-1 resistance to AZT by excision},
  author={Xiongying Tu and Kalyan Das and Qianwei Han and Joseph D. Bauman and Arthur D. Clark and Xiaorong Hou and Yulia Volovik Frenkel and Barbara L. Gaffney and Roger A. Jones and Paul L. Boyer and Stephen H. Hughes and Stefan G. Sarafianos and Eddy Arnold},
  journal={Nature Structural &Molecular Biology},
Human immunodeficiency virus (HIV-1) develops resistance to 3′-azido-2′,3′-deoxythymidine (AZT, zidovudine) by acquiring mutations in reverse transcriptase that enhance the ATP-mediated excision of AZT monophosphate from the 3′ end of the primer. The excision reaction occurs at the dNTP-binding site, uses ATP as a pyrophosphate donor, unblocks the primer terminus and allows reverse transcriptase to continue viral DNA synthesis. The excision product is AZT adenosine dinucleoside tetraphosphate… CONTINUE READING
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Structural basis for the role of the K65R mutation in HIV-1 reverse transcriptase polymerization, excision antagonism, and tenofovir resistance

  • K Das
  • J. Biol. Chem. 284,
  • 2009

Crystal structures of clinically relevant Lys103Asn/Tyr181Cys double mutant HIV-1 reverse transcriptase in complexes with ATP and non-nucleoside inhibitor HBY 097

  • K Das
  • J. Mol. Biol
  • 2007

reaching the poor with research advances

  • Fauci, A. S. 25 years of HIVAIDS science
  • Cell 131, 429–432
  • 2007

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