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Literature summary for 3.1.13.2 extracted from

  • Ehteshami, M.; Beilhartz, G.L.; Scarth, B.J.; Tchesnokov, E.P.; McCormick, S.; Wynhoven, B.; Harrigan, P.R.; Goette, M.
    Connection domain mutations N348I and A360V in HIV-1 reverse transcriptase enhance resistance to 3-azido-3-deoxythymidine through both RNase H-dependent and -independent mechanisms (2008), J. Biol. Chem., 283, 22222-22232.
    View publication on PubMedView publication on EuropePMC
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Protein Variants

Protein Variants Comment Organism
M41L/D67N/L210W/T215Y/A360V mutation decreases efficiency of RNase H cleavage and increases excision of AZT in the presence of the pyrophosphate donor ATP Human immunodeficiency virus 1
M41L/D67N/L210W/T215Y/A360V/N348I/E478Q mutation decreases efficiency of RNase H cleavage and increases excision of AZT in the presence of the pyrophosphate donor ATP Human immunodeficiency virus 1
M41L/D67N/L210W/T215Y/E478Q mutation decreases efficiency of RNase H cleavage and increases excision of AZT in the presence of the pyrophosphate donor ATP Human immunodeficiency virus 1
M41L/D67N/L210W/T215Y/N348I mutation decreases efficiency of RNase H cleavage and increases excision of AZT in the presence of the pyrophosphate donor ATP Human immunodeficiency virus 1
M41L/D67N/L210W/T215Y/N348I/A360V mutant accumulates transiently formed, shorter hybrids that can rebind to reverse transcriptase before the template is irreversibly degraded Human immunodeficiency virus 1
additional information TAMs refers to mutants that contain the following amino acid substitutions M41L/D67N/L210W/T215Y. Thymidine analogue-associated mutations (TAMs) in reverse transcriptase cause resistance to 3'-azido-3'-deoxythymidine (AZT) through excision of the incorporated monophosphate Human immunodeficiency virus 1

Inhibitors

Inhibitors Comment Organism Structure
3'-azido-3'-deoxythymidine
-
 Human immunodeficiency virus 1

Organism

Organism UniProt Comment Textmining
Human immunodeficiency virus 1
-
-
-

Purification (Commentary)

Purification (Comment) Organism
heterodimeric HIV-1 reverse transcriptase (p66 and p51) are expressed and purified Human immunodeficiency virus 1

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
DNA-RNA duplex + H2O
-
 Human immunodeficiency virus 1 ?
-
 ?

Subunits

Subunits Comment Organism
More heterodimeric HIV-1 reverse transcriptase (p66 and p51) Human immunodeficiency virus 1

Synonyms

Synonyms Comment Organism
RNase H domain of HIV-1 reverse transcriptase Human immunodeficiency virus 1