ArticleProceedings of the National Academy of Sciences of the United States of America2022
De novo design of protein homodimers containing tunable symmetric protein pockets.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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15 citing papers in PubMed, 18 citations in OpenAlex.
- De novo design of a macrocycle-induced dimerization system for cellular control.Nature communications · 2026Article
- De novo design of a macrocycle induced dimerization system for cellular control.bioRxiv : the preprint server for biology · 2026Article
- Using experimental results of protein design to guide biomolecular energy-function development.PLoS computational biology · 2026Article
- Identification of Opportunistic Pathogens on the Skin of Salamanders for Use as Molecular Targets of a De Novo Design of Multitarget Anti-International journal of microbiology · 2026Article
- Design of high-affinity binders to immune modulating receptors for cancer immunotherapy.Nature communications · 2025Article
- Contextual Analysis of Scientific Publications for Advancing Writing Skills (CASPArS): Self-Learning for Science Writing Using Top Scientists' Literature.Journal of chemical education · 2025Article
- De novo design of proteins housing excitonically coupled chlorophyll special pairs.Nature chemical biology · 2024Article
- Design of High Affinity Binders to Convex Protein Target Sites.bioRxiv : the preprint server for biology · 2024Article
- The role of cryptic ancestral symmetry in histone folding mechanisms across Eukarya and Archaea.PLoS computational biology · 2024Article
- Directing polymorph specific calcium carbonate formation with de novo protein templates.Nature communications · 2023Article
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- Design of Diverse Asymmetric Pockets inBiochemistry · 2023Article
- De Novo Design and Synthesis of Polypeptide Immunomodulators for Resetting Macrophage Polarization.Biodesign research · 2023Article
- De novo design of protein homodimers containing tunable symmetric protein pockets.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
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Authors and funding
11 authors at 4 institutions in 1 country.
Funding
Abstract
Function follows form in biology, and the binding of small molecules requires proteins with pockets that match the shape of the ligand. For design of binding to symmetric ligands, protein homo-oligomers with matching symmetry are advantageous as each protein subunit can make identical interactions with the ligand. Here, we describe a general approach to designing hyperstable C2 symmetric proteins with pockets of diverse size and shape. We first designed repeat proteins that sample a continuum of curvatures but have low helical rise, then docked these into C2 symmetric homodimers to generate an extensive range of C2 symmetric cavities. We used this approach to design thousands of C2 symmetric homodimers, and characterized 101 of them experimentally. Of these, the geometry of 31 were confirmed by small angle X-ray scattering and 2 were shown by crystallographic analyses to be in close agreement with the computational design models. These scaffolds provide a rich set of starting points for binding a wide range of C2 symmetric compounds.
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