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Mol Cell. 2001 Sep;8(3):633-44.

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

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  • 1Biotechnology Research Institute, NRC, 6100 Royalmount Avenue, Montreal, Quebec H4P 2R2, Canada.


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 calnexin family of chaperones interacts with monoglucosylated glycoproteins.

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