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Literature summary for 3.1.26.13 extracted from

  • Seckler, J.; Howard, K.; Barkley, M.; Wintrode, P.
    Solution structural dynamics of HIV-1 reverse transcriptase heterodimer (2009), Biochemistry, 48, 7646-7655.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
separate expression of subunits in Escherichia coli Human immunodeficiency virus 1

Crystallization (Commentary)

Crystallization (Comment) Organism
solution structural dynamics. Enzyme is an asymmetric heterodimer of two subunits, p66 and p51. The two subunits have the same N-terminal sequence, with the p51 subunit lacking the C-terminal RNase H domain. The p66 subunit contains the polymerase and RNase H catalytic sites. H/D exchange indicates that the RNase H domain of p66 is very flexible Human immunodeficiency virus 1

Organism

Organism UniProt Comment Textmining
Human immunodeficiency virus 1 P03366
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