The reverse transcriptase of HIV‐1: from enzymology to therapeutic intervention
| Autor: | Leila Sarih-Cottin, G.A. Nevinsky, Laura Tarrago-Litvak, Marie-Line Andreola, Simon Litvak |
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| Rok vydání: | 1994 |
| Předmět: |
biology
DNA polymerase Protein subunit RNA RNA-Directed DNA Polymerase biology.organism_classification Biochemistry Virology HIV Reverse Transcriptase Virus Reverse transcriptase Structure-Activity Relationship chemistry.chemical_compound Retrovirus chemistry Genetics biology.protein Humans Reverse Transcriptase Inhibitors RNase H Molecular Biology DNA Biotechnology |
| Zdroj: | The FASEB Journal. 8:497-503 |
| ISSN: | 1530-6860 0892-6638 |
| DOI: | 10.1096/fasebj.8.8.7514143 |
| Popis: | The human immunodeficiency virus type 1 (HIV-1) is the etiologic agent of AIDS. Replication of this virus requires the activity of a retrovirus encoded RNA-dependent DNA polymerase, or reverse transcriptase (RT). HIV-1 RT is required for the synthesis of the double-stranded proviral DNA from the single-stranded retroviral RNA genome. HIV-1 RT has two subunits of 66 kDa and 51 kDa. The 66-kDa subunit contains the DNA polymerase and RNase H domains whereas the 51-kDa subunit, obtained by proteolytic maturation of the former subunit, has only the DNA synthetic activity. Two recently reported crystal structures of HIV-1 RT have revealed the very asymmetric structure of this molecule. In addition to providing information concerning the mechanism of nucleic acid polymerization, biochemical and biophysical studies of this enzyme are providing key insights for the design of selective antiviral agents. The multiple activities displayed by reverse transcriptase in the replication of the retroviral genome ensure that this enzyme will remain at the forefront of antiviral strategies in the fight against AIDS and other retrovirus-related pathologies. |
| Databáze: | OpenAIRE |
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