![]() The domain contains two characteristic repeats 1 (-I-x-D-P-(D/E)-(A/D)-x-K-P-(E/D)-D-W-D-(D/E)-) and 2 (-G-x-W-x-x-P-x-I-x-N-P-x-Y-), and the sets are repeated four times in CNX, and three times in CRT. The P-domain shows a characteristic structure with an extended and curved arm connected to a globular N-domain. The N-domain, a globular -sandwich domain with homology to legume lectin, has been modeled based on crystallographic data for CNX. Based on structural and functional studies, CNX/CRT can be divided into three distinct domains N-terminal, proline-rich, and C-terminal (Fig. Both are monomeric, calcium-binding proteins, and are related members of the legume lectin family. CRT, another homologous ER resident, is a 55-60 kDa soluble protein with the C-terminal amino acid sequence -K-D-E-L, a retrieval signal in the ER. These also suggest that CNX and CRT play distinct biological roles in the cell.ĬNX is an 88-90 kDa transmembrane protein of type I in the ER. ![]() Gene knockout studies demonstrated that CRT-knockout mice were lethal, and CNX-knockout mice showed early death with severe neural abnormalities, indicating that CNX and CRT could not compensate each function in development. In spite of similar sugar-binding specificity, CNX and CRT bind to a variety of distinct target proteins. GlycoWord / Calnexin and Calreticulin: Glycoprotein Folding by the Calnexin/Calreticulin Cycles QS-A01Ĭalnexin and Calreticulin: Glycoprotein Folding by the Calnexin/Calreticulin CycleĬalnexin (CNX) and calreticulin (CRT) are homologous lectin-like molecular chaperones that interact with newly synthesized glycoproteins through specific monoglucosylated oligosaccharides to regulate quality control of glycoproteins in the endoplasmic reticulum (ER) (1). ![]()
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