Resistance of HIV-1 reverse transcriptase against [2',5'-bis-O-(tert-butyldimethylsilyl)-3'-spiro-5''-(4''-amino-1'',2''- oxathiole-2'',2''-dioxide)] (TSAO) derivatives is determined by the mutation Glu138-->Lys on the p51 subunit.

@article{Jonckheere1994ResistanceOH,
  title={Resistance of HIV-1 reverse transcriptase against [2',5'-bis-O-(tert-butyldimethylsilyl)-3'-spiro-5''-(4''-amino-1'',2''- oxathiole-2'',2''-dioxide)] (TSAO) derivatives is determined by the mutation Glu138-->Lys on the p51 subunit.},
  author={Heidi Jonckheere and Jean-Marc Taymans and Jan Balzarini and S. Herrero Vel{\'a}zquez and Mar{\'i}a Jos{\'e} Camarasa and Jan Desmyter and Eric De Clercq and Jozef Ann{\'e}},
  journal={The Journal of biological chemistry},
  year={1994},
  volume={269 41},
  pages={25255-8}
}
Determination of the three-dimensional structure of the human immunodeficiency virus type-1 (HIV-1) reverse transcriptase (RT) has indicated a totally different folding for the 51-kDa subunit (p51) than for the 66-kDa subunit (p66). The polymerase catalytic site is located on the p66 subunit. Moreover, the HIV-1-specific RT inhibitors, also designated as the non-nucleoside RT inhibitors (NNRTIs), select for amino acid mutations that afford resistance to these compounds and are clustered in the… CONTINUE READING