TROSY-NMR reveals interaction between ERp57 and the tip of the calreticulin P-domain.

@article{Frickel2002TROSYNMRRI,
  title={TROSY-NMR reveals interaction between ERp57 and the tip of the calreticulin P-domain.},
  author={E M Frickel and Roland Riek and Ilian Jelesarov and Ari Helenius and K. Wuthrich and Lars Ellgaard},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2002},
  volume={99 4},
  pages={
          1954-9
        }
}
The lectin chaperone calreticulin (CRT) assists the folding and quality control of newly synthesized glycoproteins in the endoplasmic reticulum (ER). It interacts with ERp57, a thiol-disulfide oxidoreductase that promotes the formation of disulfide bonds in glycoproteins bound by CRT. Here, we investigated the interaction between CRT and ERp57 by using biochemical techniques and NMR spectroscopy. We found that ERp57 binds to the P-domain of calreticulin, an independently folding domain… CONTINUE READING
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Biochemistry 37, 3480–3490

  • A. Vassilakos, M. Michalak, M. A. Lehrman, D. B. Williams
  • Frickel et al. PNAS February
  • 1998

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