Structure of the HIV-1 reverse transcriptase Q151M mutant: insights into the inhibitor resistance of HIV-1 reverse transcriptase and the structure of the nucleotide-binding pocket of Hepatitis B virus polymerase.
Result: HIV-1 RT with a Q151M mutation is known to exhibit NRTI resistance (Shirasaka et al., 1993, 1995), while it remains sensitive to tenofovir and lamivudine (Iversen et al., 1996; Mbisa et al., 2011).
Result: In contrast, the relative orientations of the p66 subdomains of HIV-1 RT Q151M superposed well onto those of the closed structures (PDB entries 1dlo and 3ith; Figs.
Result: It is evident that the Q151M mutation causes a loss of the capacity to
Result: The dNTP-binding site of HIV-1 RT Q151M was compared with azidothymidine triphosphate (AZT)-bound (PDB entry 3v4i; Das et al., 2012) and tenofovir diphosphate (TNV)-bound (PDB entry 1t05; Tuske et al., 2004) HIV-1 RT structures.
HBV mutation literature information.
PMID: 
2015
Acta crystallographica. Section F, Structural biology communications
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