1JHN

Crystal Structure of the Lumenal Domain of Calnexin

Summary for 1JHN

• Entry DOI: 10.2210/pdb1jhn/pdb
• Descriptor: calnexin, CALCIUM ION (2 entities in total)
• Functional Keywords: jelly-roll, beta sandwich, chaperone
• Biological source: Canis lupus familiaris (dog)
• Cellular location: Endoplasmic reticulum membrane; Single-pass type I membrane protein: P24643
• Total number of polymer chains: 1
• Total formula weight: 48331.84

Authors

Schrag, J.D.,Bergeron, J.M.,Li, Y.,Borisova, S.,Hahn, M.,Thomas, D.Y.,Cygler, M. (deposition date: 2001-06-28, release date: 2001-10-10, Last modification date: 2011-07-13)

Primary citation

Schrag, J.D.,Bergeron, J.J.,Li, Y.,Borisova, S.,Hahn, M.,Thomas, D.Y.,Cygler, M.
The Structure of calnexin, an ER chaperone involved in quality control of protein folding.
Mol.Cell, 8:633-644, 2001

PubMed 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.

PubMed: 11583625
DOI: 10.1016/S1097-2765(01)00318-5

Experimental method

X-RAY DIFFRACTION (2.9 Å)