Ontology highlight
ABSTRACT:
SUBMITTER: Ren G
PROVIDER: S-EPMC2665069 | biostudies-literature | 2009 Apr
REPOSITORIES: biostudies-literature
Ren Guoping G Stephan Daniel D Xu Zhaohui Z Zheng Ying Y Tang Danming D Harrison Rosemary S RS Kurz Mareike M Jarrott Russell R Shouldice Stephen R SR Hiniker Annie A Martin Jennifer L JL Heras Begoña B Bardwell James C A JC
The Journal of biological chemistry 20090130 15
The ubiquitous thioredoxin fold proteins catalyze oxidation, reduction, or disulfide exchange reactions depending on their redox properties. They also play vital roles in protein folding, redox control, and disease. Here, we have shown that a single residue strongly modifies both the redox properties of thioredoxin fold proteins and their ability to interact with substrates. This residue is adjacent in three-dimensional space to the characteristic CXXC active site motif of thioredoxin fold prote ...[more]