Structure of a 16-nm cage designed by using protein oligomers.
Designing protein molecules that will assemble into various kinds of ordered materials represents an important challenge in nanotechnology. We report the crystal structure of a 12-subunit protein cage that self-assembles by design to form a tetrahedral structure roughly 16 nanometers in diameter. The strategy of fusing together oligomeric protein domains can be generalized to produce other kinds of cages or extended materials.
University of California Los Angeles Biomedical Engineering Interdepartmental Program, Los Angeles, CA 90095, USA.
Yen-Ting
YT
Lai
Duilio
D
Cascio
Todd O
TO
Yeates
D018360:Crystallography, X-Ray; D008958:Models, Molecular; D010544:Peroxidases / Q000737:chemistry*; D011487:Protein Conformation; D015202:Protein Engineering; D055503:Protein Multimerization; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D021122:Protein Subunits / Q000737:chemistry; D011506:Proteins / Q000737:chemistry*; D014763:Viral Matrix Proteins / Q000737:chemistry*
D021122:Protein Subunits; D011506:Proteins; D014763:Viral Matrix Proteins; D010544:Peroxidases; C026195:bromide peroxidase