ArticleProceedings of the National Academy of Sciences of the United States of America2015
Computational design and experimental verification of a symmetric protein homodimer.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. 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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Who cites it
15 citing papers in PubMed.
- Article
- Protein Assembly by Design.Chemical reviews · 2021Review
- Designed Artificial Protein Heterodimers With Coupled Functions Constructed Using Bio-Orthogonal Chemistry.Frontiers in chemistry · 2021Article
- Better together: building protein oligomers naturally and by design.Biochemical Society transactions · 2019Review
- Creation of artificial protein-protein interactions using α-helices as interfaces.Biophysical reviews · 2018Review
- Hierarchical design of artificial proteins and complexes toward synthetic structural biology.Biophysical reviews · 2018Review
- Significant expansion and red-shifting of fluorescent protein chromophore determined through computational design and genetic code expansion.Biophysics reports · 2018Article
- Cyclic oligomer design with de novo αβ-proteins.Protein science : a publication of the Protein Society · 2017Article
- Computational design of self-assembling cyclic protein homo-oligomers.Nature chemistry · 2017Article
- A critical analysis of computational protein design with sparse residue interaction graphs.PLoS computational biology · 2017Article
- The coming of age of de novo protein design.Nature · 2016Review
- The Folding of de Novo Designed Protein DS119 via Molecular Dynamics Simulations.International journal of molecular sciences · 2016Article
- Designed multi-stranded heme binding β-sheet peptides in membrane.Chemical science · 2016Article
- Metal-Directed Design of Supramolecular Protein Assemblies.Methods in enzymology · 2016Article
- Article
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5 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Homodimers are the most common type of protein assembly in nature and have distinct features compared with heterodimers and higher order oligomers. Understanding homodimer interactions at the atomic level is critical both for elucidating their biological mechanisms of action and for accurate modeling of complexes of unknown structure. Computation-based design of novel protein-protein interfaces can serve as a bottom-up method to further our understanding of protein interactions. Previous studies have demonstrated that the de novo design of homodimers can be achieved to atomic-level accuracy by β-strand assembly or through metal-mediated interactions. Here, we report the design and experimental characterization of a α-helix-mediated homodimer with C2 symmetry based on a monomeric Drosophila engrailed homeodomain scaffold. A solution NMR structure shows that the homodimer exhibits parallel helical packing similar to the design model. Because the mutations leading to dimer formation resulted in poor thermostability of the system, design success was facilitated by the introduction of independent thermostabilizing mutations into the scaffold. This two-step design approach, function and stabilization, is likely to be generally applicable, especially if the desired scaffold is of low thermostability.
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