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Updated: Jul 19, 2026

Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase
Published on: February 12, 2019
The Structure of calnexin, an ER chaperone involved in quality control of protein folding
J D Schrag1, J J Bergeron, Y Li
1Biotechnology Research Institute, NRC, 6100 Royalmount Avenue, Montreal, Quebec H4P 2R2, Canada. joe@bri.nrc.ca
Abstract:
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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