Author
Listed:
- Casper A. Goverde
(École Polytechnique Fédérale de Lausanne and Swiss Institute of Bioinformatics)
- Martin Pacesa
(École Polytechnique Fédérale de Lausanne and Swiss Institute of Bioinformatics)
- Nicolas Goldbach
(École Polytechnique Fédérale de Lausanne and Swiss Institute of Bioinformatics)
- Lars J. Dornfeld
(École Polytechnique Fédérale de Lausanne and Swiss Institute of Bioinformatics)
- Petra E. M. Balbi
(École Polytechnique Fédérale de Lausanne and Swiss Institute of Bioinformatics)
- Sandrine Georgeon
(École Polytechnique Fédérale de Lausanne and Swiss Institute of Bioinformatics)
- Stéphane Rosset
(École Polytechnique Fédérale de Lausanne and Swiss Institute of Bioinformatics)
- Srajan Kapoor
(University at Buffalo)
- Jagrity Choudhury
(University at Buffalo)
- Justas Dauparas
(University of Washington
University of Washington)
- Christian Schellhaas
(École Polytechnique Fédérale de Lausanne and Swiss Institute of Bioinformatics)
- Simon Kozlov
(Massachusetts Institute of Technology)
- David Baker
(University of Washington
University of Washington
University of Washington)
- Sergey Ovchinnikov
(Massachusetts Institute of Technology)
- Alex J. Vecchio
(University at Buffalo)
- Bruno E. Correia
(École Polytechnique Fédérale de Lausanne and Swiss Institute of Bioinformatics)
Abstract
De novo design of complex protein folds using solely computational means remains a substantial challenge1. 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 receptors2, 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.
Suggested Citation
Casper A. Goverde & Martin Pacesa & Nicolas Goldbach & Lars J. Dornfeld & Petra E. M. Balbi & Sandrine Georgeon & Stéphane Rosset & Srajan Kapoor & Jagrity Choudhury & Justas Dauparas & Christian Sche, 2024.
"Computational design of soluble and functional membrane protein analogues,"
Nature, Nature, vol. 631(8020), pages 449-458, July.
Handle:
RePEc:nat:nature:v:631:y:2024:i:8020:d:10.1038_s41586-024-07601-y
DOI: 10.1038/s41586-024-07601-y
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