Self-Assembly in the Ferritin Nano-Cage Protein Superfamily

International Journal of Molecular Sciences

Yu Zhang¹ 

[1] Division of Chemistry and Biology Chemistry, Nanyang Technological University, 21 Nanyang Link, Singapore 637371, Singapore; E-Mail

关键词: ferritin;    maxi-ferritin;    mini-ferritin;    self-assembly;   

DOI  :  10.3390/ijms12085406

来源: mdpi

【 摘 要 】

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.

【 授权许可】

CC BY   
© 2011 by the authors; licensee MDPI, Basel, Switzerland.