Crystallization (Comment) | Organism |
---|---|
crystal structure analysis, overview. The pyrimidinol carboxylic acids is successful crystallized with Mn2+ and the isolated HIV RNase H domain | Human immunodeficiency virus 1 |
Protein Variants | Comment | Organism |
---|---|---|
A360I/V | site-directed mutagenesis, a connection/RNase H domain mutant | Human immunodeficiency virus 1 |
A360V | naturally occuring mutant from clinical isolates, a connection/RNase H domain mutant that shows reduced RNase H activity | Human immunodeficiency virus 1 |
A371V | site-directed mutagenesis, a connection/RNase H domain mutant | Human immunodeficiency virus 1 |
N348I | naturally occuring mutant from clinical isolates, a connection/RNase H domain mutant that shows reduced RNase H activity | Human immunodeficiency virus 1 |
Q294P | site-directed mutagenesis of a residue in the catalytically inactive p54 subunit resulting in an increase in RNase H activity comparable with that of HIV-1 reverse transcriptase | Human immunodeficiency virus 2 |
Q509L | site-directed mutagenesis, a connection/RNase H domain mutant | Human immunodeficiency virus 1 |
T473C | the mutation increases the sensitivity of the enzyme for inhibitor NSC727447 by 50fold | Human immunodeficiency virus 1 |
Y181C | site-directed mutagenesis, the mutant shows resistance to non-nucleoside reverse transcriptase inhibitors | Human immunodeficiency virus 1 |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
(4-N,N-dimethylaminobenzoyl)-2-hydroxy-1-naphthyl hydrazone | specific | Human immunodeficiency virus 1 | |
2,7-dihydroxy-4-(propan-2-yl)cyclohepta-2,4,6-trien-1-one | - |
Human immunodeficiency virus 1 | |
2-(3,4-dichlorobenzyl)-5,6-dihydroxypyrimidine-4-carboxylic acid | - |
Human immunodeficiency virus 1 | |
2-amino-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide | - |
Human immunodeficiency virus 1 | |
2-hydroxyisoquinoline-1,3(2H,4H)-dione | - |
Human immunodeficiency virus 1 | |
3,4-dihydroxy-N'-[(E)-(2-methoxynaphthalen-1-yl)methylidene]benzohydrazide | - |
Human immunodeficiency virus 1 | |
ethyl (5E)-6-[1-(4-fluorobenzyl)-1H-pyrrol-2-yl]-2,4-dioxohex-5-enoate | - |
Human immunodeficiency virus 1 | |
additional information | discovery and development of bona fide RNase H inhibitors, overview | Human immunodeficiency virus 1 | |
NSC727447 | mutation T473C increases sensitivity of the enzyme for NSC727447 by 50fold | Human immunodeficiency virus 1 |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | one Mg2+ ion in the RNase H active site, required | Human immunodeficiency virus 1 | |
Mg2+ | one Mg2+ ion in the RNase H active site, required | Human immunodeficiency virus 2 |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Human immunodeficiency virus 1 | RNase H functions as an endonuclease that specifically cleaves the RNA moiety of RNA/DNA hybrids, substrate binding and reaction mechanism, overview | ? | - |
? | |
additional information | Human immunodeficiency virus 2 | RNase H functions as an endonuclease that specifically cleaves the RNA moiety of RNA/DNA hybrids, substrate binding and reaction mechanism, overview | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Human immunodeficiency virus 1 | - |
HIV-1 | - |
Human immunodeficiency virus 2 | - |
HIV-2 | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | RNase H functions as an endonuclease that specifically cleaves the RNA moiety of RNA/DNA hybrids, substrate binding and reaction mechanism, overview | Human immunodeficiency virus 1 | ? | - |
? | |
additional information | RNase H functions as an endonuclease that specifically cleaves the RNA moiety of RNA/DNA hybrids, substrate binding and reaction mechanism, overview | Human immunodeficiency virus 2 | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | the folded structure of the HIV-1 RNase H domain takes the form of a 5-stranded mixed beta-sheet flanked by four alpha helices in an asymmetric distribution, structure comparisons, overview. The p66 subunit is subdivided into three domains: the N-terminal polymerase domain, the C-terminal ribonuclease RNase H domain, and connection domain that links the two functional regions | Human immunodeficiency virus 1 |
Synonyms | Comment | Organism |
---|---|---|
HIV-1 RT-associated RNase H | - |
Human immunodeficiency virus 1 |
ribonuclease H | - |
Human immunodeficiency virus 1 |
ribonuclease H | - |
Human immunodeficiency virus 2 |
RNase H | - |
Human immunodeficiency virus 1 |
RNase H | - |
Human immunodeficiency virus 2 |
General Information | Comment | Organism |
---|---|---|
additional information | Q294 is highly conserved in HIV-2 isolates | Human immunodeficiency virus 2 |
additional information | role of RNase H activity in drug resistance, the RNase H domains can affect the susceptibility of RT to non-nucleoside reverse transcriptase inhibitors and nucleos(t)ide reverse transcriptase inhibitors. Furthermore, RNase H activity itself is implicated in the mechanism of resistance to nucleoside reverse transcriptase inhibitors such as 3'-azidodeoxythymidine, and also to non-nucleoside reverse transcriptase inhibitors such as nevirapine. RNase H exists as a domain in the larger enzyme HIV-1 reverse transcriptase, structure and function of HIV-1 RNase H, overview | Human immunodeficiency virus 1 |
physiological function | the process of reverse transcription involves the copying of the single-stranded RNA of the viral genome into double-stranded DNA. This requires that reverse transcriptase is able to act at times as a RNA-dependent DNA polymerase, a DNA-dependent DNA polymerase, and as an RNase H that cleaves the RNA of RNA/DNA hybrids. These activities are coordinated temporally and spatially. As all three of these processes are absolutely required for the successful completion of reverse transcription, role of RNase H in (+)-strand priming and in strand transfer and (-)-strand primer removal, overview | Human immunodeficiency virus 1 |
physiological function | the process of reverse transcription involves the copying of the single-stranded RNA of the viral genome into double-stranded DNA. This requires that reverse transcriptase is able to act at times as a RNA-dependent DNA polymerase, a DNA-dependent DNA polymerase, and as an RNase H that cleaves the RNA of RNA/DNA hybrids. These activities are coordinated temporally and spatially. As all three of these processes are absolutely required for the successful completion of reverse transcription, role of RNase H in (+)-strand priming and in strand transfer and (-)-strand primer removal, overview | Human immunodeficiency virus 2 |