ArticleAngewandte Chemie (International ed. in English)2020
Designed Asymmetric Protein Assembly on a Symmetric Scaffold.
Article in Angewandte Chemie (International ed. in English), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Programming interchangeable and reversible heterooligomeric protein self-assembly using a bifunctional ligand.Chemical science · 2024Article
- Straightforward model construction and analysis of multicomponent biomolecular systems in equilibrium.RSC chemical biology · 2023Article
- Dynamic Protease Activation on a Multimeric Synthetic Protein Scaffold via Adaptable DNA-Based Recruitment Domains.Angewandte Chemie (International ed. in English) · 2021Article
- Designed Asymmetric Protein Assembly on a Symmetric Scaffold.Angewandte Chemie (International ed. in English) · 2020Article
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Authors and funding
5 authors.
Funding
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Abstract
Cellular signaling is regulated by the assembly of proteins into higher-order complexes. Bottom-up creation of synthetic protein assemblies, especially asymmetric complexes, is highly challenging. Presented here is the design and implementation of asymmetric assembly of a ternary protein complex facilitated by Rosetta modeling and thermodynamic analysis. The wild-type symmetric CT32-CT32 interface of the 14-3-3-CT32 complex was targeted, ultimately favoring asymmetric assembly on the 14-3-3 scaffold. Biochemical studies, supported by mass-balance models, allowed characterization of the parameters driving asymmetric assembly. Importantly, our work reveals that both the individual binding affinities and cooperativity between the assembling components are crucial when designing higher-order protein complexes. Enzyme complementation on the 14-3-3 scaffold highlighted that interface engineering of a symmetric ternary complex generates asymmetric protein complexes with new functions.
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