Crystallization (Comment) | Organism |
---|---|
(alpha2)2 LysRS tetramer | Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
additional information | in vitro construction of the LysRS-p38 complex, overview | Homo sapiens |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
nucleus | - |
Homo sapiens | 5634 | - |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Subunits | Comment | Organism |
---|---|---|
More | in the complex with p38, LysRs shows an alpha2beta1:beta1alpha2 organization, in which a dimeric p38 scaffold holds two LysRS alpha2 dimers in a parallel configuration, overview. The structure is designed to control both retention and mobilization of LysRS from the multi-tRNA synthetase complex | Homo sapiens |
tetramer | structure of the LysRS tetramer in solution, overview | Homo sapiens |
Synonyms | Comment | Organism |
---|---|---|
LysRS | - |
Homo sapiens |
Lysyl-tRNA synthetase | - |
Homo sapiens |
General Information | Comment | Organism |
---|---|---|
additional information | human lysyl-tRNA synthetase is bound to the multi-tRNA synthetase complex, mediated by the p38 scaffold protein, the complex maintains and regulates the aminoacylation and nuclear functions of LysRS. p38 mobilizes LysRS for redirection to the nucleus to interact with the microphthalmia associated transcription factor. Each of the N-terminal 48 residues of p38 binds one LysRS dimer and, in so doing, brings two copies of the LysRS dimer into the multi-tRNA synthetase complex. Structural organization of the LysRS-p38 complex, overview | Homo sapiens |