1H, 13C and 15N resonance assignment of WHEP domains of human glutamyl-prolyl tRNA synthetase

Title
1H, 13C and 15N resonance assignment of WHEP domains of human glutamyl-prolyl tRNA synthetase
Authors
신진호Geum-Sook HwangHee-Chul AhnSunghoon Kim김기선
Keywords
WHEP; EPRS; NMR; chemical shifts
Issue Date
2015-04
Publisher
BIOMOLECULAR NMR ASSIGNMENTS
Citation
VOL 9, 25-30
Abstract
Human bifunctional glutamyl-prolyl tRNA synthetase (EPRS) contains three WHEP domains (R123) linking two catalytic domains. These three WHEP domains have been shown to be involved in protein–protein and protein–nucleic acid interactions. In translational control of gene expression, R12 repeats is known to interact with 30UTR element in mRNAs of inflammatory gene for translational control mechanisms. While, R23 repeats interacts with NSAP1, which inhibits mRNA binding. Here we present the NMR chemical shift assignments for R12 (128 amino acids) as a 14 kDa recombinant protein and whole WHEP domains R123 (208 amino acids) as a 21 kDa recombinant protein. 97 % of backbone and 98 % of side-chain assignments have been completed in R12 analysis and 93 and 92 % of backbone and side-chain, respectively, assignments have been completed in R123 analysis based upon triple-resonance experiments.
URI
http://pubs.kist.re.kr/handle/201004/49478
ISSN
18742718
Appears in Collections:
KIST Publication > Article
Files in This Item:
There are no files associated with this item.
Export
RIS (EndNote)
XLS (Excel)
XML


qrcode

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

BROWSE