ArticleStructure (London, England : 1993)2016
Domain-Swapped Dimers of Intracellular Lipid-Binding Proteins: Evidence for Ordered Folding Intermediates.
Article in Structure (London, England : 1993), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
11 citing papers in PubMed, 12 citations in OpenAlex.
- DreamFold: A World Model to efficiently generate protein folding pathways in the latent space.Protein science : a publication of the Protein Society · 2026Article
- Photoisomerization detected in a fully wavelength-tunable rhodopsin mimic system.Acta crystallographica. Section D, Structural biology · 2026Article
- Molecular analysis of 3D domain swapping in the acylphosphatase from Escherichia coli.Acta crystallographica. Section D, Structural biology · 2026Article
- Understanding domain swapping in the c-Src SH3 domain through hinge-loop mutagenesis.Acta crystallographica. Section D, Structural biology · 2025Article
- 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
- Domain swapping: a mathematical model for quantitative assessment of structural effects.FEBS open bio · 2024Article
- Regulation of Absorption and Emission in a Protein/Fluorophore Complex.ACS chemical biology · 2024Article
- 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 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
- Engineering the hCRBPII Domain-Swapped Dimer into a New Class of Protein Switches.Journal of the American Chemical Society · 2019Article
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9 authors at 1 institution in 1 country.
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Abstract
Human Cellular Retinol Binding Protein II (hCRBPII), a member of the intracellular lipid-binding protein family, is a monomeric protein responsible for the intracellular transport of retinol and retinal. Herein we report that hCRBPII forms an extensive domain-swapped dimer during bacterial expression. The domain-swapped region encompasses almost half of the protein. The dimer represents a novel structural architecture with the mouths of the two binding cavities facing each other, producing a new binding cavity that spans the length of the protein complex. Although wild-type hCRBPII forms the dimer, the propensity for dimerization can be substantially increased via mutation at Tyr60. The monomeric form of the wild-type protein represents the thermodynamically more stable species, making the domain-swapped dimer a kinetically trapped entity. Hypothetically, the wild-type protein has evolved to minimize dimerization of the folding intermediate through a critical hydrogen bond (Tyr60-Glu72) that disfavors the dimeric form.
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