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 |