Article
Conserved structural and functional properties of D-domain containing redox-active and -inactive protein disulfide isomerase-related protein chaperones.
The Journal of biological chemistry - 13 Apr 2007
Lippert Undine, Diao Daojun, Barak Naomi N, Ferrari David M
Abstract excerpt
The structure and mode of binding of the endoplasmic reticulum protein disulfide isomerase-related proteins to their substrates is currently a focus of intensive research. We have recently determined the crystal structure of the Drosophila melanogaster protein disulfide isomerase-related protein Wind and have described two essential substrate binding sites within the protein, one within the thioredoxin b-domain...
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