Literature summary for 2.7.7.49 extracted from

Muchiri, J.M.; Li, D.; Dykes, C.; Bambara, R.A.
Efavirenz stimulates HIV-1 reverse transcriptase RNase H activity by a mechanism involving increased substrate binding and secondary cleavage activity (2013), Biochemistry, 52, 4981-4990.

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Protein Variants

Protein Variants	Comment	Organism
E478Q	polymerization activity of mutant E478Q that inactivates the RNase H catalytic site is much more sensitive to efavirenz than the wild type	Human immunodeficiency virus 1
K101E/G190S/M41lL/T215Y	patient isolate. Efavirenz stimulates the RNase H of an reverse transcriptase from a patient-derived virus that is highly resistant and grows more rapidly in the presence of low concentrations of efavirenz	Human immunodeficiency virus 1

Inhibitors

Inhibitors	Comment	Organism	Structure
efavirenz	efavirenz actually stimulates wild type RNase H binding and catalytic functions, stimulating both 3' and 5'-directed RNase H activity. Efavirenz specifically promotes binding of the reverse transcriptase to RNase H substrates	Human immunodeficiency virus 1

Organism

Organism	UniProt	Comment	Textmining
Human immunodeficiency virus 1	-	-	-

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Release 2023.1 (January 2023)