Catalytic HIV-1 integrase (IN) and Ribonuclease H (RNase H) domains belong to the polynucleotidyl transferases superfamily and are characterized by highly conserved motifs that coordinate two divalent Mg2+ cations and are attractive targets for new antiviral agents. Several structural features of both domains are now available. Drugs targeting the HIV-1 IN are currently approved for anti-HIV therapy, while no drug targeting the HIV-1 RNase H function is yet available. This review describes HIV-1 IN and the RNase H function and structures, compounds targeting their active sites and dual inhibition as a new approach for drug development.

Past and future. Current drugs targeting HIV-1 integrase and reverse transcriptase-associated ribonuclease H activity: single and dual active site inhibitors

ESPOSITO, FRANCESCA;TRAMONTANO, ENZO
2014-01-01

Abstract

Catalytic HIV-1 integrase (IN) and Ribonuclease H (RNase H) domains belong to the polynucleotidyl transferases superfamily and are characterized by highly conserved motifs that coordinate two divalent Mg2+ cations and are attractive targets for new antiviral agents. Several structural features of both domains are now available. Drugs targeting the HIV-1 IN are currently approved for anti-HIV therapy, while no drug targeting the HIV-1 RNase H function is yet available. This review describes HIV-1 IN and the RNase H function and structures, compounds targeting their active sites and dual inhibition as a new approach for drug development.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11584/98201
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