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Literature summary for 3.1.26.13 extracted from

  • Himmel, D.M.; Maegley, K.A.; Pauly, T.A.; Bauman, J.D.; Das, K.; Dharia, C.; Clark, A.D.; Ryan, K.; Hickey, M.J.; Love, R.A.; Hughes, S.H.; Bergqvist, S.; Arnold, E.
    Structure of HIV-1 reverse transcriptase with the inhibitor beta-thujaplicinol bound at the RNase H active site (2009), Structure, 17, 1625-1635.
    View publication on PubMedView publication on EuropePMC
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Crystallization (Commentary)

Crystallization (Comment) Organism
2.80 A and 2.04 A resolution crystal structures of inhibitor, beta-thujaplicinol, bound at the RNase H active site of both HIV-1 RT and an isolated RNase H domain. beta-Thujaplicinol chelates two divalent metal ions at the RNase H active site Human immunodeficiency virus 1

Inhibitors

Inhibitors Comment Organism Structure
beta-thujaplicinol slow-binding RNase H inhibitor with noncompetitive kinetics that forms a tropylium ion that interacts favorably with reverse transcriptase and the RNA:DNA substrate Human immunodeficiency virus 1

Organism

Organism UniProt Comment Textmining
Human immunodeficiency virus 1 P03366
-
-

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.00014
-
 beta-thujaplicinol presence of Mg2+ and DNA:RNA hybrid, pH 8.0 Human immunodeficiency virus 1