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Mapping of a Substrate Binding Site in the Protein Disulfide Isomerase-related Chaperone Wind Based on Protein Function and Crystal Structure
2004
Journal of Biological Chemistry
The protein disulfide isomerase (PDI)-related protein Wind is essential in Drosophila melanogaster, and is required for correct targeting of Pipe, an essential Golgi transmembrane 2-O-sulfotransferase. Apart from a thioredoxin fold domain present in all PDI proteins, Wind also has a unique C-terminal D-domain found only in PDI-D proteins. Here, we show that Pipe processing requires dimeric Wind, which interacts directly with the soluble domain of Pipe in vitro, and we map an essential substrate
doi:10.1074/jbc.m406839200
pmid:15252019
fatcat:whxx2zau45fm7mfwdxzplze6ga