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Self-assembly in the ferritin nano-cage protein superfamily Zhang Y; Orner BPInt J Mol Sci 2011[]; 12 (8): 5406-21Protein 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.|*Protein Multimerization[MESH]|Carrier Proteins/*chemistry/metabolism[MESH]|Ferritins/*chemistry/metabolism[MESH]|Hydrogen-Ion Concentration[MESH]|Macromolecular Substances/chemistry/metabolism[MESH]|Models, Molecular[MESH]|Protein Binding[MESH]|Protein Conformation[MESH] |
