title: Structural characterization of human aminoacyl-tRNA synthetases for translational and nontranslational functions.
abstract: Aminoacyl-tRNA synthetases (aaRSs) are enzymes that function at the first step of translation, catalyzing the conjugation of amino acids to their cognate tRNAs for protein synthesis. While preserving this essential role, higher eukaryotic aaRSs, such as human cytoplasmic aaRSs, have developed other functions during evolution, including angiogenesis, inflammation, development, tumorigenesis, etc. These translational and nontranslational functions of aaRSs are attractive targets for developing antibacterial, antifungal, anticancer agents and for treating other human diseases. Structural characterization of aaRS functions in both categories has deepened our understanding and provided insightful platform for further structure-based drug design. The convergence of the mechanism of action, together with their divergent functions, offers a possible protocol for studying these features of aaRSs in general. To guide this objective in future, we provide here a review on the methods used in structural analysis, which may be applied to study this special group of housekeeping proteins.
authors.affiliation: State Key Laboratory of Bioorganic and Natural Products Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, 345 Lingling Road, Shanghai 200032, China. Electronic address: fangpengfei@sioc.ac.cn.
authors.forename: Pengfei
authors.initials: P
authors.lastname: Fang
authors.affiliation: State Key Laboratory of Bioorganic and Natural Products Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, 345 Lingling Road, Shanghai 200032, China; Kangma BioTech Co., Ltd., 781 Cailun Road, Shanghai 201203, China. Electronic address: guomin@healthcodon.com.
authors.forename: Min
authors.initials: M
authors.lastname: Guo
mesh_terms: D045744:Cell Line, Tumor; D003001:Cloning, Molecular; D018360:Crystallography, X-Ray / Q000379:methods; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D015870:Gene Expression; D005822:Genetic Vectors / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D008214:Lymphocytes / Q000737:chemistry / Q000166:cytology / Q000201:enzymology; D008239:Lysine / Q000737:chemistry* / Q000378:metabolism; D008250:Lysine-tRNA Ligase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D008958:Models, Molecular; D009687:Nuclear Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D010766:Phosphorylation; D011499:Protein Processing, Post-Translational; D012357:RNA, Transfer, Lys / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism
chemical_list: C575685:AIMP2 protein, human; D009687:Nuclear Proteins; D012357:RNA, Transfer, Lys; D011994:Recombinant Proteins; D008250:Lysine-tRNA Ligase; D008239:Lysine
keywords: Aminoacyl-tRNA synthetase; LysRS; Protein purification; Structure biology