Backbone assignment of the anticodon binding domain of human Glycyl-tRNA synthetase

Abstract

Backbone 1H, 13C and 15N resonance assignments are presented for the anticodon binding domain (residues 557-674) of human glycyl-tRNA synthetase (GRS). Role of the anticodon binding domain (ABD) of GRS as an anticancer ligand has recently been reported and its role in other diseases like Charcot–Marie–Tooth (CMT) and polymyositis have increased its interest. NMR assignments were completed using the isotope [13C/15N]-enriched protein and chemical shifts based secondary structure analysis with TALOS+ demonstrate similar secondary structure as reported in X-ray structure PDB 2ZT8, except some C-terminal residues. NMR signals from the N-terminal residues 557 to 571 and 590 to 614 showed very weak or no signals exhibiting dynamics or conformational exchange in NMR timescale.