6I6H
Crystal structure of the KDEL receptor in the peptide bound state
Summary for 6I6H
| Entry DOI | 10.2210/pdb6i6h/pdb |
| Related | 6I6B |
| Descriptor | ER lumen protein-retaining receptor 2, AEKDEL peptide, (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate, ... (4 entities in total) |
| Functional Keywords | intracellular protein receptor, membrane protein, kdel, erd2 |
| Biological source | Gallus gallus (Chicken) More |
| Total number of polymer chains | 2 |
| Total formula weight | 28621.98 |
| Authors | Braeuer, P.,Newstead, S. (deposition date: 2018-11-15, release date: 2019-02-27, Last modification date: 2024-01-24) |
| Primary citation | Brauer, P.,Parker, J.L.,Gerondopoulos, A.,Zimmermann, I.,Seeger, M.A.,Barr, F.A.,Newstead, S. Structural basis for pH-dependent retrieval of ER proteins from the Golgi by the KDEL receptor. Science, 363:1103-1107, 2019 Cited by PubMed Abstract: Selective export and retrieval of proteins between the endoplasmic reticulum (ER) and Golgi apparatus is indispensable for eukaryotic cell function. An essential step in the retrieval of ER luminal proteins from the Golgi is the pH-dependent recognition of a carboxyl-terminal Lys-Asp-Glu-Leu (KDEL) signal by the KDEL receptor. Here, we present crystal structures of the chicken KDEL receptor in the apo ER state, KDEL-bound Golgi state, and in complex with an antagonistic synthetic nanobody (sybody). These structures show a transporter-like architecture that undergoes conformational changes upon KDEL binding and reveal a pH-dependent interaction network crucial for recognition of the carboxyl terminus of the KDEL signal. Complementary in vitro binding and in vivo cell localization data explain how these features create a pH-dependent retrieval system in the secretory pathway. PubMed: 30846601DOI: 10.1126/science.aaw2859 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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