![]() ![]() It also recommends further studying the formation of the intracellular complex of CNX/CRT with peptidyl-prolyl cis- trans isomerases and protein disulfide isomerase family proteins in order to understand the involvement of these proteins in glycoprotein quality control mechanism. This review discusses partner proteins interacting with calnexin and calreticulin and their functions. 1 Altmetric Metrics Abstract Calnexin (Cnx) and calreticulin (Crt), which are important chaperones in the endoplasmic reticulum (ER), participate in the folding and quality control of client. In recent years, it has been shown that proteins other than ERp57 also complex with chaperones, suggesting that there may be multiple chaperone-binding partner molecules. 2.60.120.200 1 hit 2.10.250.10 Calreticulin/calnexin, P domain 1 hit. ERp57, a disulfide isomerase family protein, complexes with these chaperones and assists in the formation of disulfide bonds. Calnexin, calreticulin, and ERp57 : Teammates in glycoprotein folding Ellgaard, Lars Frickel, Eva-Maria In: Cell Biochemistry and Biophysics, 2003, vol. These chaperones interact with nascent proteins modified with the Glc 1Man 9GlcNAc 2 (G1M9) glycan, leading to the formation of a correct structure. Calnexin and calreticulin, which are lectin-type molecular chaperones, play important roles in glycoprotein folding. Glycoprotein quality control in the endoplasmic reticulum is achieved by multiple molecular chaperones, glycosyltransferases, and glycosidases. Calreticulin and calnexin are Ca 2+-binding proteins with chaperone activity in the endoplasmic reticulum. ![]()
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