Mini-TrpRS is essential for IFNγ-induced monocyte-derived giant cell formation.
Sign Up to like & getrecommendations! Published in 2021 at "Cytokine"
DOI: 10.1016/j.cyto.2021.155486
Abstract: Truncated tryptophanyl-tRNA synthetase (mini-TrpRS), like any other aminoacyl-tRNA synthetases, canonically functions as a protein synthesis enzyme. Here we provide evidence for an additional signaling role of mini-TrpRS in the formation of monocyte-derived multinuclear giant cells… read more here.
Keywords: trprs; ifn; formation; mini trprs ... See more keywords
An alternative conformation of human TrpRS suggests a role of zinc in activating non-enzymatic function
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DOI: 10.1080/15476286.2017.1377868
Abstract: ABSTRACT Tryptophanyl-tRNA synthetase (TrpRS) in vertebrates contains a N-terminal extension in front of the catalytic core. Proteolytic removal of the N-terminal 93 amino acids gives rise to T2-TrpRS, which has potent anti-angiogenic activity mediated through… read more here.
Keywords: zinc; trprs; human trprs; conformation ... See more keywords
An asymmetric structure of bacterial TrpRS supports the half-of-the-sites catalytic mechanism and facilitates antimicrobial screening
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DOI: 10.1093/nar/gkad278
Abstract: Abstract Tryptophanyl-tRNA synthetase (TrpRS) links tryptophan to tRNATrp, thereby playing an indispensable role in protein translation. Unlike most class I aminoacyl-tRNA synthetases (AARSs), TrpRS functions as a homodimer. Herein, we captured an ‘open-closed’ asymmetric structure… read more here.
Keywords: asymmetric structure; half sites; catalytic mechanism; trprs ... See more keywords