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 HIV Protease

HIV PR (EC: is a homodimer with each subunit containing 99 residues, and active site residing in between the two identical subunits. The replication of the HIV requires a viral aspartyl protease called HIV protease (HIV PR) to cleave the virally-encoded gag and gag-pol polyproteins. This in turn releases enzymes and structural proteins that are essential for the assembly of infectious viral particles. Inhibition of HIV protease activity in infected cells leads to the production of an immature, noninfectious virus and disrupting its ability to replicate, which makes the HIV protease an attractive target for developing anti-viral agents.[ HIV PR has been a prime target for drug therapy. HIV PR inhibitors work by specifically binding to the active site by mimicking the tetrahedral intermediate of its substrate and essentially becoming “stuck,” disabling the enzyme. ]. To minimize the chance of Drug Resistance of HIV should composed the combination of multiple drugs called 'Drug Cocktail', which inhibit different activity of HIV proteins at a time.


  More Resource:   Other links:

secondary structure prediction - http://npsa-pbil.ibcp.fr/cgi-bin/npsa_automat.pl?page=/NPSA/npsa_seccons.html

peptide cutter - http://expasy.org/tools/peptidecutter/