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

Citation
Jd. Schrag et al., The structure of calnexin, an ER chaperone involved in quality control of protein folding, MOL CELL, 8(3), 2001, pp. 633-644
Citations number
53
Categorie Soggetti
Cell & Developmental Biology
Journal title
MOLECULAR CELL
ISSN journal
10972765 → ACNP
Volume
8
Issue
3
Year of publication
2001
Pages
633 - 644
Database
ISI
SICI code
1097-2765(200109)8:3<633:TSOCAE>2.0.ZU;2-C
Abstract
The three-dimensional structure of the lumenal domain of the lectin-like ch aperone calnexin determined to 2.9 Angstrom resolution reveals an extended 140 Angstrom arm inserted into a beta sandwich structure characteristic of legume lectins. The arm is composed of tandem repeats of two proline-rich s equence motifs which interact with one another in a head-to-tail fashion. I dentification of the ligand binding site establishes calnexin as a monovale nt lectin, providing insight into the mechanism by which the calnexin famil y of chaperones interacts with monoglucosylated glycoproteins.