Αποτελέσματα Αναζήτησης
Proteases from HIV cleave three polyproteins which result into various functional HIV proteins and HIV enzymes. Cleavage of polyproteins completes the maturation and release of new infective virions. This step is also an interesting target to stop HIV replication.
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.
16 Μαρ 2012 · For almost 25 years, key components of the lentivirus HIV-1, including the envelope glycoproteins, the capsid and the replication enzymes reverse transcriptase, integrase and protease, have...
HIV-1 protease (HIV-1 PR) is a dimeric enzyme from the family of aspartic proteases. The enzyme has been widely exploited as a drug target and exhibits broad substrate recognition. HIV-1 protease can be detected through designed interactions with multiple peptide sensors (Fig. 7.8; Herpoldt et al., 2015). An energy transfer can happen between ...
One of these targets is HIV-1 protease (HIV PR), an essential enzyme needed in the proper assembly and maturation of infectious virions. Understanding the chemical mechanism of this enzyme has been a basic requirement in the development of efficient inhibitors.
The function of HIV protease is to cleave the initial polyprotein into its functional constituents (Sussman et al., 2013). This enzyme is made up of a dimer of identical subunits that mimics the two-lobed monomeric structure of pepsin and other aspartate proteases.
Over the past 23 years, key components of the lentivirus HIV-1, including its envelope glycoproteins and capsid, and the replication enzymes reverse transcriptase, integrase and protease, have accordingly been scrutinized to near atomic scale resolution.
