![]() Subsequently, the two C-terminal domain helices interlock with each other to render a coiled-coil bundle and lead to the dimerization of SAS-6. In particular, two helices and five β-strands of them are packed into an N-terminal globular domain, whereas a long α-helix and two β-strands constitute the C-terminal domain. For example, the spindle assembly abnormal protein 6 (SAS-6), an essential component in the centrioles, is folded to be a central seven-stranded antiparallel open twisted β-sheet flanked by three α-helices ( Hilbert et al., 2013). Three length scales of the hierarchy are frequently involved in the evolution of sophisticated biologically relevant hierarchical organization: the folding of a linear polypeptide into a well-defined secondary and tertiary structure, the nanocluster organization of proteins driven by intermolecular forces, and the arrangement of protein-nanoclusters into macroscopic superlattices. As a matter of fact, nearly all of the structural proteins are identified to be polymers containing hundreds to millions of subunits, and most of the soluble proteins as well as membrane proteins are oligomers of two or more subunits ( Harding and Hancock, 2008 Himanen et al., 2010 Nussinov et al., 2015). The self-assembly of proteins into an enormous range of molecular machines and structural scaffolds is one of the core principles for nature to create countless organisms, such as the oligomerization of protein kinases, transmembrane proteins, and signaling proteins, the polymerization of cytoskeletal proteins into intermediate filaments, and the emergence of membrane-less organelles induced by the phase separation of proteins ( Nussinov et al., 2015 Boeynaems et al., 2018). The emergent applications of protein assemblies as versatile platforms in medicine and material science with improved performances have also been discussed. We elucidate various innovative strategies for manipulating proteins to self-assemble into desired architectures. This review outlines recent efforts directed to the creation of structurally defined protein assemblies including one-dimensional (1D) strings/rings/tubules, two-dimensional (2D) planar sheets and three-dimensional (3D) polyhedral scaffolds. Sophisticated protein self-assemblies have attracted great scientific interests due to their potential applications in disease diagnosis, illness treatment, biomechanics, bio-optics and bio-electronics, etc. 2Department of Chemistry, University of Wisconsin-Madison, Madison, WI, United Statesĭiverse natural/artificial proteins have been used as building blocks to construct a variety of well-ordered nanoscale structures over the past couple of decades.1State Key Laboratory of Medical Molecular Biology, Institute of Basic Medical Sciences, Department of Biophysics and Structural Biology, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing, China.Wenbo Zhang 1 †, Shanshan Mo 1 †, Mingwei Liu 1 †, Lei Liu 2, Lanlan Yu 1 * and Chenxuan Wang 1 *
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