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• W2025344323 abstract "Integrase is an essential retroviral enzyme that binds both termini of linear viral DNA and inserts them into a host cell chromosome. The structure of full-length retroviral integrase, either separately or in complex with DNA, has been lacking. Furthermore, although clinically useful inhibitors of HIV integrase have been developed, their mechanism of action remains speculative. Here we present a crystal structure of full-length integrase from the prototype foamy virus in complex with its cognate DNA. The structure shows the organization of the retroviral intasome comprising an integrase tetramer tightly associated with a pair of viral DNA ends. All three canonical integrase structural domains are involved in extensive protein–DNA and protein–protein interactions. The binding of strand-transfer inhibitors displaces the reactive viral DNA end from the active site, disarming the viral nucleoprotein complex. Our findings define the structural basis of retroviral DNA integration, and will allow modelling of the HIV-1 intasome to aid in the development of antiretroviral drugs. The integrase protein of retroviruses such as HIV-1 catalyses insertion of the viral genome into the host's, where the virus is able to persist in a cell indefinitely. As integration is critical for viral replication, integrase has been a target for drug development, and several inhibitors — including raltegravir and elvitegravir — are used therapeutically or are undergoing clinical trial. The search for new antiretroviral drugs has been hampered by the lack of a structure of the integrase complex (or intasome) on substrate DNA. Now the crystal structure of full-length retroviral integrase from the non-pathogenic retrovirus known as prototype foamy virus has been determined, in complex with its cognate viral DNA. As well as revealing details of the biochemistry of the integration reaction, the structure shows how current inhibitors affect this process. The integrase protein of retroviruses such as HIV-1 catalyses insertion of the viral genome into that of the host. Here, the long-awaited structure of the full-length integrase complex is predicted, revealing not only details of the biochemistry of the integration reaction, but also the means by which current inhibitors affect this process." @default.
• W2025344323 created "2016-06-24" @default.
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• W2025344323 date "2010-01-31" @default.
• W2025344323 modified "2023-10-16" @default.
• W2025344323 title "Retroviral intasome assembly and inhibition of DNA strand transfer" @default.
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• W2025344323 doi "https://doi.org/10.1038/nature08784" @default.
• W2025344323 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2837123" @default.
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