The thioredoxin-like fold: hidden domains in protein disulfide isomerases and other chaperone proteins.
Although 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.
Clissold
Patricia M
PM
Molecular Angiogenesis Laboratory, Cancer Research UK, University of Oxford, John Radcliffe Hospital, Oxford OX3 9DS, UK.
Bicknell
Roy
R
D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D017173:Caenorhabditis elegans; D019992:Databases as Topic; D004330:Drosophila; D018507:Gene Expression Regulation, Developmental; D015894:Genome, Human; D006801:Humans; D018832:Molecular Chaperones / Q000737:chemistry*; D008969:Molecular Sequence Data; D019704:Protein Disulfide-Isomerases / Q000737:chemistry*; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid; D013879:Thioredoxins / Q000737:chemistry*
D018832:Molecular Chaperones; D013879:Thioredoxins; D019704:Protein Disulfide-Isomerases