5v8z

Crystal structure of ERp29 D-domain in complex with the P-domain of calmegin

spinqualitylabelsall models 5v8z, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5v8z is a 4 chain structure with sequence from Canis lupus familiaris and Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.105Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ERP29_HUMAN Does not seem to be a disulfide isomerase. Plays an important role in the processing of secretory proteins within the endoplasmic reticulum (ER), possibly by participating in the folding of proteins in the ER. Publication Abstract from PubMed The lectin chaperones calreticulin (CRT) and calnexin (CNX) contribute to the folding of glycoproteins in the ER by recruiting foldases such as the protein disulfide isomerase ERp57 and the peptidyl prolyl cis-trans isomerase CypB. Recently, CRT was shown to interact with the chaperone ERp29. Here, we show that ERp29 directly binds to the P domain of CNX. Crystal structures of the D domain of ERp29 in complex with the P domains from CRT and calmegin, a tissue-specific CNX homolog, reveal a commonality in the mechanism of binding whereby the tip of the P domain functions as a plurivalent adapter to bind a variety of folding factors. We show that mutation of a single residue, D348 in CNX, abrogates binding to ERp29 as well as ERp57 and CypB. The structural diversity of the accessory factors suggests that these chaperones became specialized for glycoprotein folding through convergent evolution of their P-domain binding sites. Mapping the ER Interactome: The P Domains of Calnexin and Calreticulin as Plurivalent Adapters for Foldases and Chaperones.,Kozlov G, Munoz-Escobar J, Castro K, Gehring K Structure. 2017 Sep 5;25(9):1415-1422.e3. doi: 10.1016/j.str.2017.07.010. PMID:28877505 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also ER-resident protein

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