Crystal structure of the carbohydrate recognition domain of p58/ERGIC-53, a protein involved in glycoprotein export from the endoplasmic reticulum
LM Velloso, K Svensson, G Schneider… - Journal of Biological …, 2002 - ASBMB
p58/ERGIC-53 is an animal calcium-dependent lectin that cycles between the endoplasmic
reticulum (ER) and the Golgi complex and appears to act as a cargo receptor for a subset of
soluble glycoproteins exported from the ER. We have determined the crystal structure of the
carbohydrate recognition domain (CRD) of p58, the rat homologue of human ERGIC-53, to
1.46 Å resolution. The fold and ligand binding site are most similar to those of leguminous
lectins. The structure also resembles that of the CRD of the ER folding chaperone calnexin …
reticulum (ER) and the Golgi complex and appears to act as a cargo receptor for a subset of
soluble glycoproteins exported from the ER. We have determined the crystal structure of the
carbohydrate recognition domain (CRD) of p58, the rat homologue of human ERGIC-53, to
1.46 Å resolution. The fold and ligand binding site are most similar to those of leguminous
lectins. The structure also resembles that of the CRD of the ER folding chaperone calnexin …
