User:Christian Fjeld/Sandbox 1

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General Description

spinqualitylabelsall models LARS (E coli) ternary complex with tRNAleu and leucyl adenylate analogue Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Leucyl tRNA synthetase (LARS) is a 97 kDa, class IA aminoacyl-tRNA synthetase (ARS) that catalyzes the ligation of leucine with tRNAleu in an ATP dependent mechanism. LARS is a cytoplasmic enzyme that is found as part of the multisynthetase complex in mammals[1]. LARS has been shown to be involved with the mTOR pathways as a sensor of leucine levels within the cell[2]. Mutations in LARS2, the mitochondrial version of the enzyme, have been linked to Perrault syndrome characterized by premature ovarian failure in females and progressive hearing loss in both sexes[3] Contents 1 Structure 1.1 Catalytic Domain 1.2 Editing Domain 1.3 Anticodon Binding Domain 2 Disease Structure Catalytic Domain Editing Domain Anticodon Binding Domain Disease

3D Structure of LARS

Updated on 30-April-2018

References

1. ↑ Mirande M. The Aminoacyl-tRNA Synthetase Complex. Subcell Biochem. 2017;83:505-522. doi: 10.1007/978-3-319-46503-6_18. PMID:28271488 doi:http://dx.doi.org/10.1007/978-3-319-46503-6_18
2. ↑ Han JM, Jeong SJ, Park MC, Kim G, Kwon NH, Kim HK, Ha SH, Ryu SH, Kim S. Leucyl-tRNA synthetase is an intracellular leucine sensor for the mTORC1-signaling pathway. Cell. 2012 Apr 13;149(2):410-24. doi: 10.1016/j.cell.2012.02.044. Epub 2012 Mar, 15. PMID:22424946 doi:http://dx.doi.org/10.1016/j.cell.2012.02.044
3. ↑ Pierce SB, Gersak K, Michaelson-Cohen R, Walsh T, Lee MK, Malach D, Klevit RE, King MC, Levy-Lahad E. Mutations in LARS2, encoding mitochondrial leucyl-tRNA synthetase, lead to premature ovarian failure and hearing loss in Perrault syndrome. Am J Hum Genet. 2013 Apr 4;92(4):614-20. doi: 10.1016/j.ajhg.2013.03.007. Epub, 2013 Mar 28. PMID:23541342 doi:http://dx.doi.org/10.1016/j.ajhg.2013.03.007