Journal
MOLECULAR CELL
Volume 8, Issue 3, Pages 633-644Publisher
CELL PRESS
DOI: 10.1016/S1097-2765(01)00318-5
Keywords
-
Categories
Ask authors/readers for more resources
The three-dimensional structure of the lumenal domain of the lectin-like chaperone 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 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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available