Investigating the 'steric gate' of human immunodeficiency virus type 1 (HIV-1) reverse transcriptase by targeted insertion of unnatural amino acids

Five HIV-1 reverse transcriptase variants containing tyrosine analogues at position 115 of their p66 subunit are evaluated. The findings are discussed within the context of detailed structural models of HIV-1 reverse transcriptase ternary complexes containing this amino acid substitution that reveal probable mechanisms of the observed catalytic rate changes.