¹H, ¹³C, and ¹⁵N NMR resonance assignments of reduced full length and shortened forms of the Grx domain of Mus musculus TGR

Biomol NMR Assign. 2012 Apr;6(1):103-7. doi: 10.1007/s12104-011-9335-0. Epub 2011 Sep 8.

Abstract

Two forms of the glutaredoxin (Grx) domain (full length Grx domain and short Grx lacking the N-terminal region) of Mus musculus thioredoxin glutathione reductase (TGR) were isotopically labelled with (15)N and (13)C isotopes, expressed and purified to homogeneity. We report here the (1)H, (13)C and (15)N NMR assignment for both Grx forms of this mouse TGR. This investigation represents the first NMR analysis of a mammalian TGR.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Glutathione Reductase / chemistry*
  • Mice
  • Nuclear Magnetic Resonance, Biomolecular*
  • Protein Structure, Tertiary
  • Thioredoxin-Disulfide Reductase

Substances

  • Glutathione Reductase
  • Thioredoxin-Disulfide Reductase
  • Txnrd3 protein, mouse