title: Backbone ¹H, ¹³C, and ¹⁵N chemical shift assignment for HIV-1 protease subtypes and multi-drug resistant variant MDR 769.
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 (1)H, (13)C, and (15)N 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.
authors: Department of Chemistry, University of Florida, PO Box 117200, Gainesville, FL 32611, USA.
authors: Xi
authors: X
authors: Huang
authors: Ian Mitchelle S
authors: IM
authors: de Vera
authors: Angelo M
authors: AM
authors: Veloro
authors: James R
authors: JR
authors: Rocca
authors: Carlos
authors: C
authors: Simmerling
authors: Ben M
authors: BM
authors: Dunn
authors: Gail E
authors: GE
authors: Fanucci
mesh_terms: D000595:Amino Acid Sequence; D002247:Carbon Isotopes; D018432:Drug Resistance, Multiple; D024882:Drug Resistance, Viral; D016333:HIV Protease / Q000737:chemistry*; D015497:HIV-1 / Q000201:enzymology*; D008969:Molecular Sequence Data; D050505:Mutant Proteins / Q000737:chemistry*; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary; D011522:Protons
chemical_list: D002247:Carbon Isotopes; D050505:Mutant Proteins; D009587:Nitrogen Isotopes; D011522:Protons; D016333:HIV Protease; C514803:p16 protease, Human immunodeficiency virus 1