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.
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