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User:Christian Fjeld/Sandbox 1
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== General Description == | == General Description == | ||
| - | <StructureSection load='4aq7' frame='true' size='340' side='right' caption='LARS (''E coli'') ternary complex with tRNA''leu'' and leucyl adenylate analogue' scene=''> | + | <StructureSection load='4aq7' frame='true' size='340' side='right' scene='78/786656/Lars/1' caption='LARS (''E coli'') ternary complex with tRNA''leu'' and leucyl adenylate analogue' scene=''> |
Leucyl tRNA synthetase (LARS) is a 97 kDa, class IA aminoacyl-tRNA synthetase (ARS) that catalyzes the ligation of leucine with tRNA<sup>leu</sup> in an ATP dependent mechanism. LARS is a cytoplasmic enzyme that is found as part of the multisynthetase complex in mammals<ref>doi: 10.1007/978-3-319-46503-6_18</ref>. | Leucyl tRNA synthetase (LARS) is a 97 kDa, class IA aminoacyl-tRNA synthetase (ARS) that catalyzes the ligation of leucine with tRNA<sup>leu</sup> in an ATP dependent mechanism. LARS is a cytoplasmic enzyme that is found as part of the multisynthetase complex in mammals<ref>doi: 10.1007/978-3-319-46503-6_18</ref>. | ||
Revision as of 21:18, 30 April 2018
General Description
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3D Structure of LARS
Updated on 30-April-2018
References
- ↑ 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
