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The development of a modified DNA aptamer that binds HIV‐1 reverse transcriptase (RT) with ultra‐high affinity has enabled the X‐ray structure determination of an HIV‐1 RT‐DNA complex to 2.3 Å resolution without the need for an antibody Fab fragment or RT‐DNA cross‐linking. The 38‐mer hairpin‐DNA aptamer has a 15 base‐pair duplex, a three‐deoxythymidine hairpin loop, and a five‐nucleotide 5′‐overhang...
The human immunodeficiency virus type-1 (HIV-1) reverse transcriptase (RT) functions as a heterodimer (p51/p66), which makes disruption of subunit interactions a possible target for antiviral drug design. Our understanding of subunit interface interactions has been limited by the lack of virus-based approaches for studying the heterodimer. Therefore, we developed a novel subunit-specific mutagenesis...
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