ArticleIUCrJ2019
Computational design of symmetrical eight-bladed β-propeller proteins.
Article in IUCrJ, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 36 citations in OpenAlex.
- Modular protein frameworks via supramolecular synthons.Biophysical reviews · 2025Review
- Why we are made of proteins and nucleic acids: Structural biology views on extraterrestrial life.Biophysics and physicobiology · 2023Article
- Computational Design of Miniprotein Binders.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Biochemical, biophysical, and functional characterisation of the E3 ubiquitin ligase APC/C regulator CDC20 fromFrontiers in physiology · 2022Article
- Protein Design with Deep Learning.International journal of molecular sciences · 2021Review
- Structure and stability of the designer protein WRAP-T and its permutants.Scientific reports · 2021Article
- Influence of circular permutations on the structure and stability of a six-fold circular symmetric designer protein.Protein science : a publication of the Protein Society · 2020Article
- Harnessing Conformational Plasticity to Generate Designer Enzymes.Journal of the American Chemical Society · 2020Review
- Development and applications of artificial symmetrical proteins.Computational and structural biotechnology journal · 2020Review
- Molecular assemblies built with the artificial protein Pizza.Journal of structural biology: X · 2020Article
- Structural diversity of oligomeric β-propellers with different numbers of identical blades.eLife · 2019Article
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
β-Propeller proteins form one of the largest families of protein structures, with a pseudo-symmetrical fold made up of subdomains called blades. They are not only abundant but are also involved in a wide variety of cellular processes, often by acting as a platform for the assembly of protein complexes. WD40 proteins are a subfamily of propeller proteins with no intrinsic enzymatic activity, but their stable, modular architecture and versatile surface have allowed evolution to adapt them to many vital roles. By computationally reverse-engineering the duplication, fusion and diversification events in the evolutionary history of a WD40 protein, a perfectly symmetrical homologue called Tako8 was made. If two or four blades of Tako8 are expressed as single polypeptides, they do not self-assemble to complete the eight-bladed architecture, which may be owing to the closely spaced negative charges inside the ring. A different computational approach was employed to redesign Tako8 to create Ika8, a fourfold-symmetrical protein in which neighbouring blades carry compensating charges. Ika2 and Ika4, carrying two or four blades per subunit, respectively, were found to assemble spontaneously into a complete eight-bladed ring in solution. These artificial eight-bladed rings may find applications in bionanotechnology and as models to study the folding and evolution of WD40 proteins.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.