Abstract
HIV-1 protease (HIV-1PR) is an essential drug target in the treatment of patients infected with HIV-1. Mutations are found to arise in over 38 of 99 amino acid sites in this protein in response to drug therapy or natural selection, where many are found combinations that alter enzyme kinetics or inhibitor susceptibility without a clear structural mechanism. In efforts to understand how these mutations alter the flexibility and dynamics of HIV-1PR, we report the backbone 1H, 13C, and 15N chemical shift assignments for subtypes C, circulating recombinant form CRF01_AE and a multi-drug resistant variant MDR 769. These assignments are essential for future work aimed at characterizing backbone dynamics, exchange dynamics and dynamics of protein/substrate or protein/inhibitor interactions.
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Acknowledgments
We acknowledge Dr. Jeff F. Ellena at UVA for his help with data collection. This work is supported by NSF MBC-0746533 (GEF), UF Department of Chemistry, UF Center for AIDS Research, and by NIH grant AI28571 (BMD). Acquisition of NMR data was supported through the National High Magnetic Field Laboratory (NHMFL) and obtained at the Advanced Magnetic Resonance Imaging and Spectroscopy (AMRIS) in the McKnight Brain Institute of the University of Florida.
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Huang, X., de Vera, I.M.S., Veloro, A.M. et al. Backbone 1H, 13C, and 15N chemical shift assignment for HIV-1 protease subtypes and multi-drug resistant variant MDR 769. Biomol NMR Assign 7, 199–202 (2013). https://doi.org/10.1007/s12104-012-9409-7
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DOI: https://doi.org/10.1007/s12104-012-9409-7