title: Self-assembly in the ferritin nano-cage protein superfamily.
abstract: Protein 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.
authors.affiliation: Division of Chemistry and Biology Chemistry, Nanyang Technological University, 21 Nanyang Link, Singapore 637371, Singapore; E-Mail:  zh0010yu@e.ntu.edu.sg.
authors.forename: Yu
authors.initials: Y
authors.lastname: Zhang
authors.forename: Brendan P
authors.initials: BP
authors.lastname: Orner
mesh_terms: D002352:Carrier Proteins / Q000737:chemistry* / Q000378:metabolism; D005293:Ferritins / Q000737:chemistry* / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D046911:Macromolecular Substances / Q000737:chemistry / Q000378:metabolism; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation; D055503:Protein Multimerization
chemical_list: D002352:Carrier Proteins; D046911:Macromolecular Substances; D005293:Ferritins