1jhn
From Proteopedia
Crystal Structure of the Lumenal Domain of Calnexin
Overview
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.
About this Structure
1JHN is a Single protein structure of sequence from Canis lupus familiaris. Full crystallographic information is available from OCA.
Reference
The Structure of calnexin, an ER chaperone involved in quality control of protein folding., Schrag JD, Bergeron JJ, Li Y, Borisova S, Hahn M, Thomas DY, Cygler M, Mol Cell. 2001 Sep;8(3):633-44. PMID:11583625 Page seeded by OCA on Fri May 2 21:14:03 2008
