title: ¹H, ¹³C, and ¹⁵N NMR resonance assignments of reduced full length and shortened forms of the Grx domain of Mus musculus TGR.
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.
authors: Department of Biotechnology, Norwegian University of Science and Technology, Sem Sælands vei 6/8, 7491 Trondheim, Norway.
authors: Elena
authors: E
authors: Shumilina
authors: Alice
authors: A
authors: Soldà
authors: Maxim
authors: M
authors: Gerashchenko
authors: Vadim N
authors: VN
authors: Gladyshev
authors: Alexander
authors: A
authors: Dikiy
mesh_terms: D000818:Animals; D005980:Glutathione Reductase / Q000737:chemistry*; D051379:Mice; D019906:Nuclear Magnetic Resonance, Biomolecular; D017434:Protein Structure, Tertiary; D013880:Thioredoxin-Disulfide Reductase
chemical_list: D005980:Glutathione Reductase; D013880:Thioredoxin-Disulfide Reductase; C424443:Txnrd3 protein, mouse