ArticleProtein science : a publication of the Protein Society2020
Design and structure of two new protein cages illustrate successes and ongoing challenges in protein engineering.
Article in Protein science : a publication of the Protein Society, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- Self-assembling protein cages: from coiled-coil module to machine learning-drivenMaterials advances · 2026Review
- A suite of designed protein cages using machine learning and protein fragment-based protocols.Structure (London, England : 1993) · 2024Article
- X-ray crystal structure of a designed rigidified imaging scaffold in the ligand-free conformation.Acta crystallographica. Section F, Structural biology communications · 2024Article
- Design of a symmetry-broken tetrahedral protein cage by a method of internal steric occlusion.Protein science : a publication of the Protein Society · 2024Article
- An interaction network approach predicts protein cage architectures in bionanotechnology.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Design of a symmetry-broken tetrahedral protein cage by a method of internal steric occlusion.bioRxiv : the preprint server for biology · 2023Article
- A Suite of Designed Protein Cages Using Machine Learning Algorithms and Protein Fragment-Based Protocols.bioRxiv : the preprint server for biology · 2023Article
- Article
- Cryo-EM structure determination of small therapeutic protein targets at 3 Å-resolution using a rigid imaging scaffold.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Design of Beta-2 Microglobulin Adsorbent Protein Nanoparticles.Biomolecules · 2023Article
- Design, synthesis, and characterization of protein origami based on self-assembly of a brick and staple artificial protein pair.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Dissecting the general mechanisms of protein cage self-assembly by coarse-grained simulations.Protein science : a publication of the Protein Society · 2023Article
- Engineered Protein Nanocages for Concurrent RNA and Protein Packaging In Vivo.ACS synthetic biology · 2022Article
- De novo designed protein inhibitors of amyloid aggregation and seeding.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Computational Design of Single-Peptide Nanocages with Nanoparticle Templating.Molecules (Basel, Switzerland) · 2022Article
- Protein Assembly by Design.Chemical reviews · 2021Review
- Bioengineering bacterial encapsulin nanocompartments as targeted drug delivery system.Synthetic and systems biotechnology · 2021Article
- Artificial Organelles: Towards Adding or Restoring Intracellular Activity.Chembiochem : a European journal of chemical biology · 2021Review
- Structure-based design of novel polyhedral protein nanomaterials.Current opinion in microbiology · 2021Review
- Engineering spatiotemporal organization and dynamics in synthetic cells.Wiley interdisciplinary reviews. Nanomedicine and nanobiotechnology · 2021Review
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8 authors.
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Abstract
In recent years, new protein engineering methods have produced more than a dozen symmetric, self-assembling protein cages whose structures have been validated to match their design models with near-atomic accuracy. However, many protein cage designs that are tested in the lab do not form the desired assembly, and improving the success rate of design has been a point of recent emphasis. Here we present two protein structures solved by X-ray crystallography of designed protein oligomers that form two-component cages with tetrahedral symmetry. To improve on the past tendency toward poorly soluble protein, we used a computational protocol that favors the formation of hydrogen-bonding networks over exclusively hydrophobic interactions to stabilize the designed protein-protein interfaces. Preliminary characterization showed highly soluble expression, and solution studies indicated successful cage formation by both designed proteins. For one of the designs, a crystal structure confirmed at high resolution that the intended tetrahedral cage was formed, though several flipped amino acid side chain rotamers resulted in an interface that deviates from the precise hydrogen-bonding pattern that was intended. A structure of the other designed cage showed that, under the conditions where crystals were obtained, a noncage structure was formed wherein a porous 3D protein network in space group I2
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