Member database | SUPERFAMILY |
SUPERFAMILY type | homologous superfamily |
Description Imported from IPR009033
The type-I integral membrane protein calnexin (CNX) and its soluble paralog calreticulin (CRT) are members of a family of molecular chaperones that function in the endoplasmic reticulum (ER) of eukaryotic cells. These calcium-binding proteins are lectins that bind newly synthesised N-linked glycoproteins to help promote efficient folding and oligomeric assembly. The chaperones act to retain the glycoproteins in the ER while they are still incompletely folded, ensuring that the ER quality control machinery can dispose of misfolded glycoproteins. The family of molecular chaperones are conserved among plants, fungi, and animals.
References Imported from IPR009033
1. NMR structure of the calreticulin P-domain. Ellgaard L, Riek R, Herrmann T, Guntert P, Braun D, Helenius A, Wuthrich K. Proc. Natl. Acad. Sci. U.S.A. 98, 3133-8, (2001). View articlePMID: 11248044
2. 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 8, 633-44, (2001). View articlePMID: 11583625
Integrated to
External Links
Representative structure
3ici: Crystal structure of cyclophilin B in complex with calmegin fragment