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Literature summary for 2.7.7.49 extracted from

  • Miller, M.; Tuske, S.; Das, K.; DeStefano, J.; Arnold, E.
    Structure of HIV-1 reverse transcriptase bound to a novel 38-mer hairpin template-primer DNA aptamer (2016), Protein Sci., 25, 46-55 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
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Human immunodeficiency virus 1

Crystallization (Commentary)

Crystallization (Comment) Organism
the development of a modified DNA aptamer that binds HIV-1 reverse transcriptase (RT) with ultra-high affinity enables the X-ray structure determination of an HIV-1 RT-DNA complex to 2.3 A resolution without the need for an antibody Fab fragment or RT-DNA crosslinking. The 38-mer hairpin-DNA aptamer has a 15 base-pair duplex, a three-deoxythymidine hairpin loop, and a five-nucleotide 5'-overhang. The aptamer binds RT in a template-primer configuration with the 3'-end positioned at the polymerase active site and has 2'-O-methyl modificationsat the second and fourth duplex template nucleotides that interact with the p66 fingers and palm subdomains. This structure represents the highest resolution RT-nucleic acid structure to date. The RT-aptamer complex is catalytically active and can serve as a platform for studying fundamental RT mechanisms and for development of anti-HIV inhibitors through fragment screening and other approaches Human immunodeficiency virus 1

Organism

Organism UniProt Comment Textmining
Human immunodeficiency virus 1 P03366 group M subtype B, isolate BH10
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Purification (Commentary)

Purification (Comment) Organism
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Human immunodeficiency virus 1

Synonyms

Synonyms Comment Organism
reverse transcriptase
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Human immunodeficiency virus 1