ArticleChemistry & biology2015
Engineered Domain Swapping as an On/Off Switch for Protein Function.
Article in Chemistry & biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
21 citing papers in PubMed.
- SplitSeek-Pro: accurate prediction of splittable sites on protein structures.Nature communications · 2026Article
- Insights into mechanisms and significance of domain swapping from emerging examples in the Mog1p/PsbP-like fold.Biochemical and biophysical research communications · 2025Review
- Domain swapping: a mathematical model for quantitative assessment of structural effects.FEBS open bio · 2024Article
- Strategies for Conditional Regulation of Proteins.JACS Au · 2023Review
- Enhancing response of a protein conformational switch by using two disordered ligand binding domains.Frontiers in molecular biosciences · 2023Article
- AlphaFold accurately predicts distinct conformations based on the oligomeric state of a de novo designed protein.Protein science : a publication of the Protein Society · 2022Article
- Engineering protein and DNA tools for creating DNA-dependent protein switches.Methods in enzymology · 2022Article
- Toward Microbial Recycling and Upcycling of Plastics: Prospects and Challenges.Frontiers in microbiology · 2022Review
- Protein Assembly by Design.Chemical reviews · 2021Review
- Testing the length limit of loop grafting in a helical repeat protein.Current research in structural biology · 2021Article
- 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
- Monothiol and dithiol glutaredoxin-1 fromIUCrJ · 2020Article
- Engineering protein assemblies with allosteric control via monomer fold-switching.Nature communications · 2019Article
- Engineering the hCRBPII Domain-Swapped Dimer into a New Class of Protein Switches.Journal of the American Chemical Society · 2019Article
- Tandem domain swapping: determinants of multidomain protein misfolding.Current opinion in structural biology · 2019Review
- A Single Protein Disruption Site Results in Efficient Reassembly by Multiple Engineering Methods.Biophysical journal · 2019Article
- A five-residue motif for the design of domain swapping in proteins.Nature communications · 2019Article
- Converting a Periplasmic Binding Protein into a Synthetic Biosensing Switch through Domain Insertion.BioMed research international · 2019Review
- Amino-acid composition after loop deletion drives domain swapping.Protein science : a publication of the Protein Society · 2017Article
- Understanding protein domain-swapping using structure-based models of protein folding.Progress in biophysics and molecular biology · 2017Review
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Domain swapping occurs when identical proteins exchange segments in reciprocal fashion. Natural swapping mechanisms remain poorly understood, and engineered swapping has the potential for creating self-assembling biomaterials that encode for emergent functions. We demonstrate that induced swapping can be used to regulate the function of a target protein. Swapping is triggered by inserting a "lever" protein (ubiquitin) into one of four loops of the ribose binding protein (RBP) target. The lever splits the target, forcing RBP to refold in trans to generate swapped oligomers. Identical RBP-ubiquitin fusions form homo-swapped complexes with the ubiquitin domain acting as the hinge. Surprisingly, some pairs of non-identical fusions swap more efficiently with each other than they do with themselves. Nuclear magnetic resonance experiments reveal that the hinge of these hetero-swapped complexes maps to a region of RBP distant from both ubiquitins. This design is expected to be applicable to other proteins to convert them into functional switches.
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Registered trials
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.