ArticleNature communications2019
A five-residue motif for the design of domain swapping in proteins.
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 19 papers.
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Who cites it
19 citing papers in PubMed.
- Examining Genetic Variants Associated with FOXP1 Syndrome through Molecular Dynamics of Its DNA-Binding Domain and Self-Organizing Maps.Journal of chemical information and modeling · 2026Article
- Smolstatin1, a unique cystatin-like stefin ofCurrent research in microbial sciences · 2026Article
- Structure-Based Insights into Stefin-Mediated Targeting of Fowlerpain-1: Towards Novel Therapeutics forPharmaceuticals (Basel, Switzerland) · 2025Article
- Insights into mechanisms and significance of domain swapping from emerging examples in the Mog1p/PsbP-like fold.Biochemical and biophysical research communications · 2025Review
- Design of a light and CaProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Experimental and Computational Studies on Domain-Swapped Structure Stabilization of an Antibody Light Chain by Disulfide Bond Introduction.Journal of medicinal chemistry · 2024Article
- Oxidative Stress and Cataract Formation: Evaluating the Efficacy of Antioxidant Therapies.Biomolecules · 2024Review
- Article
- A single-domain protein catenane of dihydrofolate reductase.National science review · 2023Article
- The HIV-1 Gag Protein Displays Extensive Functional and Structural Roles in Virus Replication and Infectivity.International journal of molecular sciences · 2022Review
- 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
- Article
- Protein Assembly by Design.Chemical reviews · 2021Review
- Experimental and theoretical study on converting myoglobin into a stable domain-swapped dimer by utilizing a tight hydrogen bond network at the hinge region.RSC advances · 2021Article
- Human DND1-RRM2 forms a non-canonical domain swapped dimer.Protein science : a publication of the Protein Society · 2021Article
- Resources and Methods for Engineering "Designer" Glycan-Binding Proteins.Molecules (Basel, Switzerland) · 2021Review
- Testing the length limit of loop grafting in a helical repeat protein.Current research in structural biology · 2021Article
- Article
- Tandem domain swapping: determinants of multidomain protein misfolding.Current opinion in structural biology · 2019Review
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Domain swapping is the process by which identical monomeric proteins exchange structural elements to generate dimers/oligomers. Although engineered domain swapping is a compelling strategy for protein assembly, its application has been limited due to the lack of simple and reliable design approaches. Here, we demonstrate that the hydrophobic five-residue 'cystatin motif' (QVVAG) from the domain-swapping protein Stefin B, when engineered into a solvent-exposed, tight surface loop between two β-strands prevents the loop from folding back upon itself, and drives domain swapping in non-domain-swapping proteins. High-resolution structural studies demonstrate that engineering the QVVAG stretch independently into various surface loops of four structurally distinct non-domain-swapping proteins enabled the design of different modes of domain swapping in these proteins, including single, double and open-ended domain swapping. These results suggest that the introduction of the QVVAG motif can be used as a mutational approach for engineering domain swapping in diverse β-hairpin proteins.
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