9BEI
Cryo-EM structure of synthetic claudin-4 complex with Clostridium perfringens enterotoxin C-terminal domain, sFab COP-2, and Nanobody
This is a non-PDB format compatible entry.
Summary for 9BEI
| Entry DOI | 10.2210/pdb9bei/pdb |
| Related | 7DTM |
| EMDB information | 44479 |
| Descriptor | Claudin-4, Heat-labile enterotoxin B chain, COP-2 Fab Heavy chain, ... (5 entities in total) |
| Functional Keywords | claudin, fab, toxin, membrane protein, membrane protein-immune sysytem complex, membrane protein/immune sysytem |
| Biological source | Clostridium perfringens More |
| Total number of polymer chains | 5 |
| Total formula weight | 98625.79 |
| Authors | Vecchio, A.J. (deposition date: 2024-04-15, release date: 2024-04-24, Last modification date: 2024-10-16) |
| Primary citation | Goverde, C.A.,Pacesa, M.,Goldbach, N.,Dornfeld, L.J.,Balbi, P.E.M.,Georgeon, S.,Rosset, S.,Kapoor, S.,Choudhury, J.,Dauparas, J.,Schellhaas, C.,Kozlov, S.,Baker, D.,Ovchinnikov, S.,Vecchio, A.J.,Correia, B.E. Computational design of soluble and functional membrane protein analogues. Nature, 631:449-458, 2024 Cited by PubMed Abstract: De novo design of complex protein folds using solely computational means remains a substantial challenge. Here we use a robust deep learning pipeline to design complex folds and soluble analogues of integral membrane proteins. Unique membrane topologies, such as those from G-protein-coupled receptors, are not found in the soluble proteome, and we demonstrate that their structural features can be recapitulated in solution. Biophysical analyses demonstrate the high thermal stability of the designs, and experimental structures show remarkable design accuracy. The soluble analogues were functionalized with native structural motifs, as a proof of concept for bringing membrane protein functions to the soluble proteome, potentially enabling new approaches in drug discovery. In summary, we have designed complex protein topologies and enriched them with functionalities from membrane proteins, with high experimental success rates, leading to a de facto expansion of the functional soluble fold space. PubMed: 38898281DOI: 10.1038/s41586-024-07601-y PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.16 Å) |
Structure validation
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