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8FLX

De novo designed homotrimer; the fusion product of BGL17 and DHR59

Summary for 8FLX
Entry DOI10.2210/pdb8flx/pdb
DescriptorLK031 (1 entity in total)
Functional Keywordsde novo, computationally designed, designed, tandem repeat protein, de novo protein, kibloid, homotrimer
Biological sourcesynthetic construct
Total number of polymer chains1
Total formula weight38677.87
Authors
Kibler, R.D.,Kennedy, M.A.,Stoddard, B.L.,Lee, S. (deposition date: 2022-12-22, release date: 2023-06-28, Last modification date: 2025-01-01)
Primary citationLee, S.,Kibler, R.D.,Ahn, G.,Hsia, Y.,Borst, A.J.,Philomin, A.,Kennedy, M.A.,Huang, B.,Stoddard, B.,Baker, D.
Four-component protein nanocages designed by programmed symmetry breaking.
Nature, 2024
Cited by
PubMed Abstract: Four, eight or twenty C3 symmetric protein trimers can be arranged with tetrahedral, octahedral or icosahedral point group symmetry to generate closed cage-like structures. Viruses access more complex higher triangulation number icosahedral architectures by breaking perfect point group symmetry, but nature appears not to have explored similar symmetry breaking for tetrahedral or octahedral symmetries. Here we describe a general design strategy for building higher triangulation number architectures starting from regular polyhedra through pseudosymmetrization of trimeric building blocks. Electron microscopy confirms the structures of T = 4 cages with 48 (tetrahedral), 96 (octahedral) and 240 (icosahedral) subunits, each with 4 distinct chains and 6 different protein-protein interfaces, and diameters of 33 nm, 43 nm and 75 nm, respectively. Higher triangulation number viruses possess very sophisticated functionalities; our general route to higher triangulation number nanocages should similarly enable a next generation of multiple antigen-displaying vaccine candidates and targeted delivery vehicles.
PubMed: 39695226
DOI: 10.1038/s41586-024-07814-1
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (4.5 Å)
Structure validation

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