Similarities and differences in the thioredoxin superfamily

• Type: Another Publication in an International Scientific Journal
• Date: 2006

Authors

Carvalho, AP (Author) Other; Fernandes, PA (Author) FCUP; Ramos, MJ (Author) FCUP

Journal

Title: PROGRESS IN BIOPHYSICS & MOLECULAR BIOLOGY

Vol. 91

Pages: 229-248

ISSN: 0079-6107

Publisher: Elsevier

Indexing

ISI Web of Knowledge - 98 Citations

Scopus - 96 Citations

Scientific classification

FOS: Natural sciences > Biological sciences

Other information

Authenticus ID: P-004-K1V

DOI: 10.1016/j.pbiomolbio.2005.06.012

Abstract (EN): There is growing interest in the proteins involved in protein folding. This is mainly due to the large number of human diseases related to defects in folding, which include cystic fibrosis, Alzheimer's and cancer. However, equally important as the oxidation and concomitant formation of disulfide bridges of the extracellular or secretory proteins is the reduction and maintenance in the reduced state of the proteins within the cell. Interestingly, the proteins that are responsible for maintenance of the reduced state belong to the same superfamily as those responsible for the formation of disulfide bridges: all are members of the thioredoxin superfamily. In this article, we highlight the main features of those thioredoxin-like proteins directly involved in the redox reactions. We describe their biological functions, cytoplasmic location, mechanisms of action, structures and active site features, and discuss the principal hypotheses concerning origins of the different reduction potentials and unusual pK(a)'s of the catalytic residues.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 20