5V8Z
Crystal structure of ERp29 D-domain in complex with the P-domain of calmegin
Summary for 5V8Z
| Entry DOI | 10.2210/pdb5v8z/pdb |
| Related | 5V90 |
| Descriptor | Endoplasmic reticulum resident protein 29, Calmegin (3 entities in total) |
| Functional Keywords | chaperone, protein binding, protein folding |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 4 |
| Total formula weight | 32492.45 |
| Authors | Kozlov, G.,Munoz-Escobar, J.,Gehring, K. (deposition date: 2017-03-22, release date: 2017-06-21, Last modification date: 2023-10-04) |
| Primary citation | Kozlov, G.,Munoz-Escobar, J.,Castro, K.,Gehring, K. Mapping the ER Interactome: The P Domains of Calnexin and Calreticulin as Plurivalent Adapters for Foldases and Chaperones. Structure, 25:1415-1422.e3, 2017 Cited by PubMed Abstract: 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. PubMed: 28877505DOI: 10.1016/j.str.2017.07.010 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.105 Å) |
Structure validation
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