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The catalytic domain features an RNaseH-type fold in the superfamily of polynucleotidyl transferases, with an active site containing two Asp residues and one Glu forming the DDE motif essential for catalysis. Criteria to confirm integrase as the drug target includes activity against recombinant integrase, accumulation of 2-LTR circles in treated cells, emergence of drug-resistant virus mutations, and drug inactivity in biochemical assays on mutated integrases.DKAs, DCQ acids, DCT acids, PDP, SQL, Quinolone derived.
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The catalytic domain has an RNaseH-type fold and belongs to the superfamily of polynucleotidyl transferases. The active site is comprised of two Asp residues and one Glu, in the typical DDE motif, each of which is required for catalysis.
four criteria to conclude that integrase is theinhibitor target: 1. found to be active against recombinant integrase. 2. infected cells treated with the drug must show an accumulation of 2-LTR circles, resulting from the accumulation of viral cDNA and decreased HIV integration into host 3. integrase mutations must be found in drug-resistant viruses 4, the drug should be inactive in biochemical assays against recombinantintegrases bearing the mutations identified in the drug-resistant viruses DKAs DCQ acids; DCT acids PDP SQL Quinolone derived
