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.
Abstract: Although the structure of HIV-1 RT Q151M superimposes well onto that of HIV-1 RT in a closed conformation, a slight movement of the beta-strands (beta2-beta3) that partially create the dNTP-binding pocket was observed.
Abstract: Here, the crystal structure of HIV-1 RT Q151M, determined at 2.6 A resolution, in a new crystal form with space group P321 is presented.
Abstract: The Q151M mutation in HIV-1 RT, located at the dNTP-binding site, confers resistance to various NRTIs, while maintaining sensitivity to tenofovir and lamivudine.
Abstract: The structure also highlighted the possibility that the hydrogen-bonding network among amino acids and NRTIs is rearranged by the Q151M
HBV mutation literature information.
PMID: 
2015
Acta crystallographica. Section F, Structural biology communications
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