6YWC
De novo designed protein 4E1H_95 in complex with 101F antibody
Summary for 6YWC
| Entry DOI | 10.2210/pdb6ywc/pdb |
| Descriptor | Antibody 101F, Heavy Chain, Antibody 101F, light chain, De novo design 4E1H_95, ... (4 entities in total) |
| Functional Keywords | de novo designed protein, de novo protein |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 6 |
| Total formula weight | 121449.93 |
| Authors | Yang, C.,Sesterhenn, F.,Pojer, F.,Correia, B.E. (deposition date: 2020-04-29, release date: 2020-10-07, Last modification date: 2024-11-20) |
| Primary citation | Yang, C.,Sesterhenn, F.,Bonet, J.,van Aalen, E.A.,Scheller, L.,Abriata, L.A.,Cramer, J.T.,Wen, X.,Rosset, S.,Georgeon, S.,Jardetzky, T.,Krey, T.,Fussenegger, M.,Merkx, M.,Correia, B.E. Bottom-up de novo design of functional proteins with complex structural features. Nat.Chem.Biol., 17:492-500, 2021 Cited by PubMed Abstract: De novo protein design has enabled the creation of new protein structures. However, the design of functional proteins has proved challenging, in part due to the difficulty of transplanting structurally complex functional sites to available protein structures. Here, we used a bottom-up approach to build de novo proteins tailored to accommodate structurally complex functional motifs. We applied the bottom-up strategy to successfully design five folds for four distinct binding motifs, including a bifunctionalized protein with two motifs. Crystal structures confirmed the atomic-level accuracy of the computational designs. These de novo proteins were functional as components of biosensors to monitor antibody responses and as orthogonal ligands to modulate synthetic signaling receptors in engineered mammalian cells. Our work demonstrates the potential of bottom-up approaches to accommodate complex structural motifs, which will be essential to endow de novo proteins with elaborate biochemical functions, such as molecular recognition or catalysis. PubMed: 33398169DOI: 10.1038/s41589-020-00699-x PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.85 Å) |
Structure validation
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