Viruses, 2019-07, Vol.11 (7), p.598
2019
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Details
- Autor(en) / Beteiligte
- Titel
- Structural and Functional Aspects of Foamy Virus Protease-Reverse Transcriptase
- Ist Teil von
- Viruses, 2019-07, Vol.11 (7), p.598
- Ort / Verlag
- Switzerland: MDPI AG
- Erscheinungsjahr
- 2019
- Quelle
- EZB Electronic Journals Library
- Beschreibungen/Notizen
- Reverse transcription describes the process of the transformation of single-stranded RNA into double-stranded DNA via an RNA/DNA duplex intermediate, and is catalyzed by the viral enzyme reverse transcriptase (RT). This event is a pivotal step in the life cycle of all retroviruses. In contrast to orthoretroviruses, the domain structure of the mature RT of foamy viruses is different, i.e., it harbors the protease (PR) domain at its N-terminus, thus being a PR-RT. This structural feature has consequences on PR activation, since the enzyme is monomeric in solution and retroviral PRs are only active as dimers. This review focuses on the structural and functional aspects of simian and prototype foamy virus reverse transcription and reverse transcriptase, as well as special features of reverse transcription that deviate from orthoretroviral processes, e.g., PR activation.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 1999-4915eISSN: 1999-4915DOI: 10.3390/v11070598Titel-ID: cdi_doaj_primary_oai_doaj_org_article_72736d85edf4487fb3a9bbbbb42f3d7f
- Format
- –
- Schlagworte
- antiviral drugs, Binding sites, Deoxyribonucleic acid, DNA, Double-stranded RNA, foamy virus, Gene expression, Genomes, HIV, Human immunodeficiency virus, Life cycles, N-Terminus, Peptides, protease, Proteinase, Proteins, resistance, reverse transcriptase, Reverse transcription, Review, RNA-directed DNA polymerase, RNase H, Single-stranded DNA, Structure-function relationships, Viruses