Structure and function of HIV-1 reverse transcriptase: molecular mechanisms of polymerization and inhibition.
J Mol Biol
; 385(3): 693-713, 2009 Jan 23.
Article
em En
| MEDLINE
| ID: mdl-19022262
ABSTRACT
The rapid replication of HIV-1 and the errors made during viral replication cause the virus to evolve rapidly in patients, making the problems of vaccine development and drug therapy particularly challenging. In the absence of an effective vaccine, drugs are the only useful treatment. Anti-HIV drugs work; so far drug therapy has saved more than three million years of life. Unfortunately, HIV-1 develops resistance to all of the available drugs. Although a number of useful anti-HIV drugs have been approved for use in patients, the problems associated with drug toxicity and the development of resistance means that the search for new drugs is an ongoing process. The three viral enzymes, reverse transcriptase (RT), integrase (IN), and protease (PR) are all good drug targets. Two distinct types of RT inhibitors, both of which block the polymerase activity of RT, have been approved to treat HIV-1 infections, nucleoside analogs (NRTIs) and nonnucleosides (NNRTIs), and there are promising leads for compounds that either block the RNase H activity or block the polymerase in other ways. A better understanding of the structure and function(s) of RT and of the mechanism(s) of inhibition can be used to generate better drugs; in particular, drugs that are effective against the current drug-resistant strains of HIV-1.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Biopolímeros
/
Inibidores da Transcriptase Reversa
/
Transcriptase Reversa do HIV
Idioma:
En
Revista:
J Mol Biol
Ano de publicação:
2009
Tipo de documento:
Article
País de afiliação:
Estados Unidos