Aminoacyl-tRNA synthetases: Structure, function, and drug discovery

被引:94
|
作者
Rajendran, Vijayakumar [1 ]
Kalita, Parismita [1 ]
Shukla, Harish [1 ]
Kumar, Awanish [2 ]
Tripathi, Timir [1 ]
机构
[1] North Eastern Hill Univ, Dept Biochem, Mol & Struct Biophys Lab, Shillong, Meghalaya, India
[2] Natl Inst Technol, Dept Biotechnol, Raipur, Madhya Pradesh, India
关键词
Aminoacyl-tRNA synthetase; Rossmann fold; Motif; Inhibitor; Protein synthesis; Drug discovery; GLUTAMINYL-TRANSFER-RNA; PROTEIN-PROTEIN INTERACTIONS; RIBONUCLEIC-ACID SYNTHETASE; ESCHERICHIA-COLI; BACILLUS-SUBTILIS; LACTIC-ACIDOSIS; MACROMOLECULAR ASSEMBLAGE; MULTISYNTHETASE COMPLEX; SELENOCYSTEINE SYNTHASE; SUBSTRATE RECOGNITION;
D O I
10.1016/j.ijbiomac.2017.12.157
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Aminoacyl-tRNA synthetases (AARSs) are the enzymes that catalyze the aminoacylation reaction by covalently linking an amino acid to its cognate tRNA in the first step of protein translation. Beyond this classical function, these enzymes are also known to have a role in several metabolic and signaling pathways that are important for cell viability. Study of these enzymes is of great interest to the researchers due to its pivotal role in the growth and survival of an organism. Further, unfolding the interesting structural and functional aspects of these enzymes in the last few years has qualified them as a potential drug target against various diseases. Here we review the classification, function, and the conserved as well the appended structural architecture of these enzymes in detail, including its association with multi-synthetase complexes. We also considered their role in human diseases in terms of mutations and autoantibodies against AARSs. Finally, we have discussed the available inhibitors against AARSs. This review offers comprehensive information on AARSs under a single canopy that would be a good inventory for researchers working in this area. (C) 2018 Elsevier B.V. All rights reserved.
引用
收藏
页码:400 / 414
页数:15
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