ArticleJournal of the American Chemical Society2019
Engineering the hCRBPII Domain-Swapped Dimer into a New Class of Protein Switches.
Article in Journal of the American Chemical Society, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Photoisomerization detected in a fully wavelength-tunable rhodopsin mimic system.Acta crystallographica. Section D, Structural biology · 2026Article
- Multi-epitope ligand-conjugated nanoparticles for tumor neoantigen targeting: advancing molecular precision in cancer immunotherapy.Medical oncology (Northwood, London, England) · 2025Review
- Structural dynamics and binding of Caenorhabditis elegans lifespan-extending lipid binding protein-3 to polyunsaturated fatty acids.Protein science : a publication of the Protein Society · 2025Article
- Regulation of Absorption and Emission in a Protein/Fluorophore Complex.ACS chemical biology · 2024Article
- Redox- and metal-directed structural diversification in designed metalloprotein assemblies.Chemical communications (Cambridge, England) · 2022Article
- Protein Assembly by Design.Chemical reviews · 2021Review
- Design of Large Stokes Shift Fluorescent Proteins Based on Excited State Proton Transfer of an Engineered Photobase.Journal of the American Chemical Society · 2021Article
- Orthogonal Activation of Metabotropic Glutamate Receptor Using Coordination Chemogenetics.Frontiers in chemistry · 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
- A novel 3D-printed centrifugal ultrafiltration method reveals in vivo glycation of human serum albumin decreases its binding affinity for zinc.Metallomics : integrated biometal science · 2020Article
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Authors and funding
12 authors.
Funding
Abstract
Protein conformational switches or allosteric proteins play a key role in the regulation of many essential biological pathways. Nonetheless, the implementation of protein conformational switches in protein design applications has proven challenging, with only a few known examples that are not derivatives of naturally occurring allosteric systems. We have discovered that the domain-swapped (DS) dimer of hCRBPII undergoes a large and robust conformational change upon retinal binding, making it a potentially powerful template for the design of protein conformational switches. Atomic resolution structures of the apo- and holo-forms illuminate a simple, mechanical movement involving sterically driven torsion angle flipping of two residues that drive the motion. We further demonstrate that the conformational "readout" can be altered by addition of cross-domain disulfide bonds, also visualized at atomic resolution. Finally, as a proof of principle, we have created an allosteric metal binding site in the DS dimer, where ligand binding results in a reversible 5-fold loss of metal binding affinity. The high resolution structure of the metal-bound variant illustrates a well-formed metal binding site at the interface of the two domains of the DS dimer and confirms the design strategy for allosteric regulation.
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