Structure-function studies of HIV reverse transcriptase

Vinayaka R. Prasad, S. P. Goff

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

The retroviral RT is properly under intensive study as the major target of antiviral therapy. The enzyme exhibits a number of features that make it an attractive target: it is crucial for viral replication; its RNA-dependent DNA polymerase activity is probably unique to viral replication, or if not unique, is generally unimportant in host cell function; its activities are readily monitored; and powerful lead compounds in the form of nucleotide analogues are already in hand. Our laboratory has been involved in studies to elucidate the structure and function of the HIV-1 RT and to develop a formal genetics of the enzyme. Working with constructs expressing RT in bacteria, we have been able to use in vitro mutagenesis to localize functions on the molecule; by coupling mutagenesis with high-throughput screening of colonies, we have been able to isolate mutants with specific, rare, phenotypes. We believe that extensions of these efforts will help us to understand the functions of the protein and, coupled to a detailed three-dimensional structure, should facilitate the development of new and better inhibitors.

Original languageEnglish (US)
Pages (from-to)11-21
Number of pages11
JournalAnnals of the New York Academy of Sciences
Volume616
StatePublished - 1990
Externally publishedYes

Fingerprint

HIV Reverse Transcriptase
Mutagenesis
RNA-Directed DNA Polymerase
Enzymes
Antiviral Agents
HIV-1
Nucleotides
Hand
Lead compounds
Bacteria
Phenotype
Screening
Proteins
Throughput
Molecules
Replication
AIDS/HIV
Therapeutics
Lead
In Vitro Techniques

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

Structure-function studies of HIV reverse transcriptase. / Prasad, Vinayaka R.; Goff, S. P.

In: Annals of the New York Academy of Sciences, Vol. 616, 1990, p. 11-21.

Research output: Contribution to journalArticle

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