Probing the interaction between HIV-1 protease and the homodimeric p66/p66' reverse transcriptase precursor by double electron-electron resonance EPR spectroscopy.

Probing the interaction between HIV-1 protease and the homodimeric p66/p66' reverse transcriptase precursor by double electron-electron resonance EPR spectroscopy. Chembiochem. 2020 Jun 18;: Authors: Schmidt T, Louis J, Clore GM Abstract Following excision from the Gag-Pol polyprotein, HIV-1 reverse transcriptase is released as an asymmetric homodimer comprising two structurally dissimilar but amino acid sequence identical p66 subunits. Subsequent cleavage of the RNase H domain from only one of the subunits, denoted as p66', results in the formation of the mature p66/p51 enzyme in which catalytic activity resides in the p66 subunit and the p51 subunit (derived from p66') provides a supporting structural scaffold. Here we probe the interaction of the p66/p66' asymmetric reverse transcriptase precursor with HIV-1 protease by pulsed Q-band double electron-electron resonance EPR spectroscopy to measure distances between nitroxide labels introduced at surface engineered cysteine residues. These data suggest that the flexible, exposed linker between the RNaseH and connection domains in the open state of the p66' subunit binds to the active site of protease in a configuration that is similar to that of extended peptide substrates. PMID: 32558168 [PubMed - as supplied by publisher]
Source: Chembiochem - Category: Biochemistry Authors: Tags: Chembiochem Source Type: research
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