The thioredoxin‐like fold: Hidden domains in protein disulfide isomerases and other chaperone proteins
Copyright policy )The thioredoxin‐like fold: Hidden domains in protein disulfide isomerases and other chaperone proteins
AbstractAlthough protein disulphide isomerase (PDI) has been known for nearly 40 years, several new PDIs have recently been described that reveal a remarkable diversity in both structure and function. This article reviews our current knowledge of the PDI family members and identifies four novel PDIs in the human genome. These include human transmembrane proteins that have C. elegans or Drosophila orthologues for which a developmental role has been proven. Their role in development, together with other functional roles for PDIs such as conferring resistance to apoptosis under hypoxia and a potential role in the oxygen‐sensing apparatus are discussed. Supplementary material for this article can be found on the BioEssays website (http://www.interscience.wiley.com/jpages/0265‐9247/suppmat/2003/25/v25.603.html). BioEssays 25:603–611, 2003. © 2003 Wiley Periodicals, Inc.
- University of Oxford United Kingdom
- Oxford University Hospitals NHS Trust United Kingdom
- MRC Weatherall Institute of Molecular Medicine United Kingdom
- Cancer Research UK United Kingdom
- John Radcliffe Hospital United Kingdom
Protein Folding, Binding Sites, Sequence Homology, Amino Acid, Genome, Human, Amino Acid Motifs, Molecular Sequence Data, Protein Disulfide-Isomerases, Gene Expression Regulation, Developmental, Protein Structure, Tertiary, Thioredoxins, Databases as Topic, Animals, Humans, Drosophila, Amino Acid Sequence, Caenorhabditis elegans, Molecular Chaperones
Protein Folding, Binding Sites, Sequence Homology, Amino Acid, Genome, Human, Amino Acid Motifs, Molecular Sequence Data, Protein Disulfide-Isomerases, Gene Expression Regulation, Developmental, Protein Structure, Tertiary, Thioredoxins, Databases as Topic, Animals, Humans, Drosophila, Amino Acid Sequence, Caenorhabditis elegans, Molecular Chaperones
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