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Literature summary for 6.1.1.6 extracted from

  • Fang, P.; Zhang, H.M.; Shapiro, R.; Marshall, A.G.; Schimmel, P.; Yang, X.L.; Guo, M.
    Structural context for mobilization of a human tRNA synthetase from its cytoplasmic complex (2011), Proc. Natl. Acad. Sci. USA, 108, 8239-8244.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 6.1.1.6

Crystallization (Commentary)

Crystallization (Comment) Organism
(alpha2)2 LysRS tetramer Homo sapiens

Protein Variants

Protein Variants Comment Organism
additional information in vitro construction of the LysRS-p38 complex, overview Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
nucleus
-
 Homo sapiens 5634
-

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Subunits

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

Synonyms Comment Organism
LysRS
-
 Homo sapiens
Lysyl-tRNA synthetase
-
 Homo sapiens

General Information

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