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23 Νοε 2024 · In this chapter, we present a comprehensive review of the structural and functional studies on HIV protease, including its significance in the AIDS treatment, its catalytic mechanism, subtypes, inhibitors, and the evolution of drug resistance to protease inhibitors.
HIV-1 protease or PR is a retroviral aspartyl protease (retropepsin), an enzyme involved with peptide bond hydrolysis in retroviruses, that is essential for the life-cycle of HIV, the retrovirus that causes AIDS.
11 Νοε 2008 · Our analysis identified residues both in the hydrophobic core and at the dimeric interface (DI) that are very important for the protease function. This study demonstrates a potential utility of the SNAPP method for rational design of mutagenesis studies and protein engineering.
HIV protease, the third virally encoded enzyme, is required in this step to cleave a viral polyprotein precursor into individual mature proteins. The viral RNA and viral proteins assemble at the cell surface into new virions, which then bud from the cell and are released to infect another cell.
Viral proteases are diverse in structure, oligomeric state, catalytic mechanism, and substrate specificity. This chapter focuses on proteases from viruses that are relevant to human health: human immunodeficiency virus subtype 1 (HIV-1), hepatitis C (HCV), human T-cell leukemia virus type 1 (HTLV-1), flaviviruses, enteroviruses, and coronaviruses.
1 Ιαν 2007 · The HIV‐1 protease is synthesized as part of a large Gag‐Pol precursor protein. It is responsible for its own release from the precursor and the processing of the Gag and Gag‐Pol polyproteins into the mature structural and functional proteins required for virus maturation.
HIV-1 protease performs an essential step in the life cycle of HIV. Like many viruses, HIV makes many of its proteins in one long piece, with several proteins strung together. HIV-1 protease has the job of cutting this long "polyprotein" into the proper protein-sized pieces.
