1H, 15N and 13C backbone and side‐chain assignments of reduced and S-nitrosated C62only mutant of human thioredoxin.

Autor: Almeida, Vitor S., Iqbal, Anwar, Almeida, Fabio C. L.
Zdroj: Biomolecular NMR Assignments; Oct2021, Vol. 15 Issue 2, p261-265, 5p
Abstrakt: Thioredoxins are ubiquitous and conserved small proteins. The redox-active site is composed of highly conserved Cys32 and Cys35. In higher eukaryotes, thioredoxin evolved to a gain of function in nitrosative control, with 3 extra cysteines, Cys62, Cys69, and Cys73. Human thioredoxin 1 (hTrx) is directly involved in cellular signal transduction through S-nitrosation. The understanding of the mechanism of S-nitrosation is essential. Here we produced a mutant of hTrx containing only Cys62 (C62only). We report the almost full 1H, 15N, and 13C chemical shift assignment of the reduced and S-nitrosated C62only. This study will help to measure the reactivity Cys62 toward S-nitrosants and the stability of S-nitrosated Cys62. [ABSTRACT FROM AUTHOR]
Databáze: Complementary Index
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