Backbone assignment of the anticodon binding domain of human Glycyl-tRNA synthetase
- Authors
- Ul Mushtaq, Ameeq; Cho, Hye Young; Byun, Youngjoo; Jeon, Young Ho
- Issue Date
- 6월-2016
- Publisher
- KOREAN MAGNETIC RESONANCE SOC
- Keywords
- Glycyl-tRNA synthetase; anticodon binding domain(ABD); backbone assignment
- Citation
- JOURNAL OF THE KOREAN MAGNETIC RESONANCE SOCIETY, v.20, no.2, pp.50 - 55
- Indexed
- KCI
- Journal Title
- JOURNAL OF THE KOREAN MAGNETIC RESONANCE SOCIETY
- Volume
- 20
- Number
- 2
- Start Page
- 50
- End Page
- 55
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/88553
- DOI
- 10.6564/JKMRS.2016.20.2.050
- ISSN
- 1226-6531
- Abstract
- Backbone H-1, C-13 and N-15 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.
- Files in This Item
- There are no files associated with this item.
- Appears in
Collections - College of Pharmacy > Department of Pharmaceutical Science > 1. Journal Articles
Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.