Self-Assembly in the Ferritin Nano-Cage Protein Superfamily
AbstractProtein self-assembly, through specific, high affinity, and geometrically constraining protein-protein interactions, can control and lead to complex cellular nano-structures. Establishing an understanding of the underlying principles that govern protein self-assembly is not only essential to appreciate the fundamental biological functions of these structures, but could also provide a basis for their enhancement for nano-material applications. The ferritins are a superfamily of well studied proteins that self-assemble into hollow cage-like structures which are ubiquitously found in both prokaryotes and eukaryotes. Structural studies have revealed that many members of the ferritin family can self-assemble into nano-cages of two types. Maxi-ferritins form hollow spheres with octahedral symmetry composed of twenty-four monomers. Mini-ferritins, on the other hand, are tetrahedrally symmetric, hollow assemblies composed of twelve monomers. This review will focus on the structure of members of the ferritin superfamily, the mechanism of ferritin self-assembly and the structure-function relations of these proteins.
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Zhang, Y.; Orner, B.P. Self-Assembly in the Ferritin Nano-Cage Protein Superfamily. Int. J. Mol. Sci. 2011, 12, 5406-5421.
Zhang Y, Orner BP. Self-Assembly in the Ferritin Nano-Cage Protein Superfamily. International Journal of Molecular Sciences. 2011; 12(8):5406-5421.Chicago/Turabian Style
Zhang, Yu; Orner, Brendan P. 2011. "Self-Assembly in the Ferritin Nano-Cage Protein Superfamily." Int. J. Mol. Sci. 12, no. 8: 5406-5421.