ArticleNature communications2019
Engineering protein assemblies with allosteric control via monomer fold-switching.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Association of Hemoglobin and Myoglobin into Supramolecular Complexes: Significance for Life and Practice.International journal of molecular sciences · 2025Review
- Targeting the protein folding transition state by mutation: Large scale (un)folding rate accelerations without altering native stability.Protein science : a publication of the Protein Society · 2024Article
- Slow conformational changes in the rigid and highly stable chymotrypsin inhibitor 2.Protein science : a publication of the Protein Society · 2023Article
- Redox- and metal-directed structural diversification in designed metalloprotein assemblies.Chemical communications (Cambridge, England) · 2022Article
- The stability and dynamics of computationally designed proteins.Protein engineering, design & selection : PEDS · 2022Review
- Design principles of protein switches.Current opinion in structural biology · 2022Review
- Protein Assembly by Design.Chemical reviews · 2021Review
- Reversible molecular motional switch based on circular photoactive protein oligomers exhibits unexpected photo-induced contraction.Cell reports. Physical science · 2021Article
- Synergistic stabilization of a double mutant in chymotrypsin inhibitor 2 from a library screen in E. coli.Communications biology · 2021Article
- Artificial Organelles: Towards Adding or Restoring Intracellular Activity.Chembiochem : a European journal of chemical biology · 2021Review
- Cosolute modulation of protein oligomerization reactions in the homeostatic timescale.Biophysical journal · 2021Article
- Structural stability of SARS-CoV-2 3CLpro and identification of quercetin as an inhibitor by experimental screening.International journal of biological macromolecules · 2020Article
- Human Cellular Retinol Binding Protein II Forms a Domain-Swapped Trimer Representing a Novel Fold and a New Template for Protein Engineering.Chembiochem : a European journal of chemical biology · 2020Article
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Authors and funding
12 authors.
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Abstract
The macromolecular machines of life use allosteric control to self-assemble, dissociate and change shape in response to signals. Despite enormous interest, the design of nanoscale allosteric assemblies has proven tremendously challenging. Here we present a proof of concept of allosteric assembly in which an engineered fold switch on the protein monomer triggers or blocks assembly. Our design is based on the hyper-stable, naturally monomeric protein CI2, a paradigm of simple two-state folding, and the toroidal arrangement with 6-fold symmetry that it only adopts in crystalline form. We engineer CI2 to enable a switch between the native and an alternate, latent fold that self-assembles onto hexagonal toroidal particles by exposing a favorable inter-monomer interface. The assembly is controlled on demand via the competing effects of temperature and a designed short peptide. These findings unveil a remarkable potential for structural metamorphosis in proteins and demonstrate key principles for engineering protein-based nanomachinery.
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