The Structure of calnexin, an ER chaperone involved in quality control of protein folding.

@article{Schrag2001TheSO,
  title={The Structure of calnexin, an ER chaperone involved in quality control of protein folding.},
  author={J. Schrag and J. Bergeron and Y. Li and S. Borisova and M. Hahn and D. Thomas and M. Cygler},
  journal={Molecular cell},
  year={2001},
  volume={8 3},
  pages={
          633-44
        }
}
The three-dimensional structure of the lumenal domain of the lectin-like chaperone calnexin determined to 2.9 A resolution reveals an extended 140 A arm inserted into a beta sandwich structure characteristic of legume lectins. The arm is composed of tandem repeats of two proline-rich sequence motifs which interact with one another in a head-to-tail fashion. Identification of the ligand binding site establishes calnexin as a monovalent lectin, providing insight into the mechanism by which the… Expand
368 Citations
Mutational analysis of calnexin.
  • 2
NMR structures of 36 and 73-residue fragments of the calreticulin P-domain.
  • 57
Structural Basis of Cyclophilin B Binding by the Calnexin/Calreticulin P-domain*♦
  • 79
  • PDF
Beyond lectins: the calnexin/calreticulin chaperone system of the endoplasmic reticulum
  • 409
  • PDF
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 54 REFERENCES
Lectins as chaperones in glycoprotein folding.
  • 226
Enhanced Catalysis of Ribonuclease B Folding by the Interaction of Calnexin or Calreticulin with ERp57*
  • 334
  • PDF
Conformation-Independent Binding of Monoglucosylated Ribonuclease B to Calnexin
  • 186
Cotranslational folding and calnexin binding during glycoprotein synthesis.
  • 236
  • PDF
...
1
2
3
4
5
...