Dissociation constant of the calreticulin/ERp57

Value 9 uM
Organism Budding yeast Saccharomyces cerevisiae
Reference Peaper DR, Cresswell P. Regulation of MHC class I assembly and peptide binding. Annu Rev Cell Dev Biol. 200824:pp. 350PubMed ID18729726
Primary Source Frickel EM, Riek R, Jelesarov I, Helenius A, Wuthrich K, Ellgaard L. TROSY-NMR reveals interaction between ERp57 and the tip of the calreticulin P-domain. Proc Natl Acad Sci U S A. 2002 Feb 1999(4):1954-9PubMed ID11842220
Method ELISA, Isothermal Titration Microcalorimetry (ITC),NMR spectroscopy
Comments The lectin chaperone calreticulin (CRT) assists the folding and quality control of newly synthesized glycoproteins in the endoplasmic reticulum (ER). It interacts with ERp57, a thiol-disulfide oxidoreductase that promotes the formation of disulfide bonds in glycoproteins bound by CRT.
Entered by Uri M
ID 102661