Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	De novo design of quasisymmetric two-component protein cages.
Journal, issue, pages	Nature, Year 2026
Publish date	May 20, 2026
Authors	Shunzhi Wang / Ying Xie / David Chemielewski / Connor Weidle / Tong Shu / Green Ahn / Ryan D Kibler / Cindy Hernandez / Wei Chen / David Camilo Duran / Ann Carr / Asim K Bera / Sangmin Lee / Justin Decarreau / Alex Kang / Evans Brackenbrough / Emily Joyce / Kejia Wu / Andrew J Borst / Andrew Favor / Buwei Huang / Frank DiMaio / Liam J Holt / David Baker /
PubMed Abstract	Quasisymmetric icosahedral viral capsids achieve larger sizes than possible with strictly symmetric icosahedra by tessellating pentagons and hexagons using a single subunit that adopts different ...Quasisymmetric icosahedral viral capsids achieve larger sizes than possible with strictly symmetric icosahedra by tessellating pentagons and hexagons using a single subunit that adopts different conformations in symmetrically non-equivalent locations. Recapitulating such quasisymmetric architectures through computational design is a considerable challenge in nanomaterials engineering. Here we introduce a computational design strategy based on geometric frustration to generate two-component, quasisymmetric protein cages with customizable properties. We designed complementary trimeric and dimeric protein components that co-assemble into positively curved local hexagonal assemblies. Hexagonal lattices cannot tile spherical surfaces; instead, the components form closed sphere-like cage assemblies through incorporation of curvature-inducing pentagonal defects, as evidenced by electron microscopy. By designing dimers that encode different local curvatures, we programmed cage dimensions ranging from 40 to over 200 nm in diameter and with molecular weights from 2 MDa to over 50 MDa, comparable with natural virus capsids. We further functionalized these large cages with additional protein domains to enable ribonucleoprotein cargo loading and cellular uptake. Fluorescently labelled cage assemblies expressed in mammalian cells function as rheological probes and cargo recruiters, enabling a systematic study of size-dependent cytoplasmic diffusion and protein localization. Thus, the quasi-symmetry that has long fascinated structural biologists can now be achieved by computational protein design, with immediate applications to biologics delivery and molecular cell biology.
External links	Nature / PubMed:42162421
Methods	EM (single particle) / EM (subtomogram averaging) / X-ray diffraction
Resolution	2.15 - 31.6 Å
Structure data	70605 9om3 EMDB-70605, PDB-9om3: Two Component Protein Nano-Particle (T=3). De Novo Design, Computationally Relaxed into Low Resolution Single Particle CryoEM Map with Icosahedral Symmetry Applied Method: EM (single particle) / Resolution: 17.45 Å 70685 9op9 EMDB-70685, PDB-9op9: Two Component Protein Nano-Particle (T=3). De Novo Design, Computationally Relaxed into Low Resolution Subtomogram Averaged CryoEM Map with Icosahedral Symmetry Applied Method: EM (subtomogram averaging) / Resolution: 31.6 Å PDB-9ndl: Crystal Structure of C2-B-alpha20 Method: X-RAY DIFFRACTION / Resolution: 2.15 Å
Chemicals	ChemComp-HOH: WATER
Source	synthetic construct (others)
Keywords	DE NOVO PROTEIN / design model / ML/AI / quasi symmetry / nanoparticles / Goldberg icosahedron / C60 / Fullerene