Retrovirus protease characterized as a dimeric aspartic proteinase.
AUTOR(ES)
Katoh, I
RESUMO
Retroviruses and retroviruslike elements have a protease for specific cleavage of their polyprotein precursors. On the basis of amino acid sequences conserved among species and the sensitivity to protease inhibitors, it was proposed that the retrovirus protease could be classified as an aspartic proteinase. Since the virus protease molecule is comparable to a single domain of aspartic proteinases having two symmetrical domains, we hypothesized and examined the dimer formation of the protease. The results of biochemical molecular mass determination and cross-linking experiments demonstrated that the virus protease molecules self-assemble into dimers. An inhibitory effect of fragmented protease molecules suggests the possibility that the intermolecular association is required for their activity. Other experiments of chemical inactivation suggest a close resemblance of the catalytic features of retrovirus and aspartic proteinases. Characterizations of these bovine and avian virus proteases would provide basic knowledge for the design of retrovirus protease-specific inhibitors, which is one of the possible strategies against human immunodeficiency virus infection.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=250640Documentos Relacionados
- Human immunodeficiency virus 1 protease expressed in Escherichia coli behaves as a dimeric aspartic protease.
- A Plant Chloroplast Glutamyl Proteinase.
- Characterization of a maize root proteinase.
- A second hepatitis C virus-encoded proteinase.
- Determinants of substrate recognition by poliovirus 2A proteinase.