Warning: The NCBI web site requires JavaScript to function. more...
An official website of the United States government
The .gov means it's official. Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you're on a federal government site.
The site is secure. The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.
thioredoxin domain-containing protein
thioredoxin fold domain-containing protein
disulfide isomerase DsbC N-terminal domain-containing protein
This is the N-terminal domain of the disulfide bond isomerase DsbC. The whole molecule is V-shaped, where each arm is a DsbC monomer of two domains linked by a hinge; and the N-termini of each monomer join to form the dimer interface at the base of the V, so are vital for dimerisation [1]. DsbC is required for disulfide bond formation and functions as a disulfide bond isomerase during oxidative protein-folding in bacterial periplasm. It also has chaperone activity [2]. [1]. 10700276. Crystal structure of the protein disulfide bond isomerase, DsbC,. from Escherichia coli.. McCarthy AA, Haebel PW, Torronen A, Rybin V, Baker EN, Metcalf. P;. Nat Struct Biol. 2000;7:196-199.. [2]. 16087673. Copper stress causes an in vivo requirement for the Escherichia. coli disulfide isomerase DsbC.. Hiniker A, Collet JF, Bardwell JC;. J Biol Chem. 2005;280:33785-33791. (from Pfam)
thiol:disulfide interchange protein DsbG
thiol:disulfide interchange protein DsbG is involved in disulfide bond formation, and also functions as a protein disulfide isomerase and chaperone to correct non-native disulfide bonds
Filter your results:
Your browsing activity is empty.
Activity recording is turned off.
Turn recording back on