title: 1H, 13C and 15N resonance assignment of the anticodon binding domain of human lysyl aminoacyl tRNA synthetase.
abstract: Human lysyl aminoacyl tRNA synthetase (hLysRS) is a multi-functional aminoacyl tRNA synthetase which is primarily involved in protein biosynthesis as well as crucial processes ranging from proinflammatory response to signal transduction. One important, non-canonical function of hLysRS is to target tRNA(Lys,3), the HIV-1 reverse transcription primer molecule, for uptake and packaging into new HIV-1 particles. Since the anticodon binding (ACB) domain of hLysRS is required for proper recognition of its cognate tRNA, NMR studies of the ACB domain are being conducted to enhance our understanding of how hLysRS interacts with these RNAs during protein biosysnthesis as well as HIV-1 viral packaging. Here, we report the backbone and side chain NMR resonance assignments of the uniformly (15)N-, (13)C-labeled ACB domain of hLysRS.
authors: Department of Chemistry, University of Cincinnati, 301 Clifton Court, Cincinnati, OH 45221-0172, USA.
authors: Sheng
authors: S
authors: Liu
authors: Michael
authors: M
authors: Howell
authors: Joel
authors: J
authors: Melby
authors: Pearl
authors: P
authors: Tsang
mesh_terms: D000926:Anticodon / Q000378:metabolism*; D002247:Carbon Isotopes; D006801:Humans; D008250:Lysine-tRNA Ligase / Q000737:chemistry* / Q000378:metabolism*; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular; D011485:Protein Binding; D017433:Protein Structure, Secondary; D011522:Protons
chemical_list: D000926:Anticodon; D002247:Carbon Isotopes; D009587:Nitrogen Isotopes; D011522:Protons; D008250:Lysine-tRNA Ligase