Advances in design of protein folds and assemblies. (October 2017)

• Record Type: Journal Article
• Authors: Ljubetič, Ajasja; Gradišar, Helena; Jerala, Roman
• Is Part Of: Current opinion in chemical biology. Volume 40(2017)
• Page Start: 65
• Page End: 71
• Publication Date: 2017-10
• Subjects: Bioorganic chemistry -- Periodicals; Biology -- Periodicals; Biochemistry -- Periodicals; Clinical biochemistry -- Periodicals; Biochemistry -- Periodicals; Chimie bio-organique -- Périodiques; Biologie -- Périodiques; 572.05
• DOI: 10.1016/j.cbpa.2017.06.020
• Languages: English
• ISSNs: 1367-5931

Abstract

Graphical abstract: Highlights: De novo single chain proteins can be designed with atomic accuracy. Multi-chain protein assemblies can be created based on different symmetries. Extremely large symmetric multicomponent structures can be accurately designed. Protein cages with adjustable volume and shape can be designed based on single or multiple chains. Abstract : Conceptual and computational advances triggered an explosion of designed protein structures in the recent years. Various protein fold geometries have been robustly designed with atomic accuracy, including protein folds unseen in nature. The same principles and tools have been extended to design multi-chain assemblies. By exploiting symmetry, mega-Dalton structures have been created with exciting potential applications for synthetic biology. In this review we focus on design of single chain and multi polypeptide chain assemblies of defined size and composition. Several innovative strategies have been developed to create de novo protein assemblies, with the two main approaches to the design of multi-chain assemblies being genetic fusion of interacting modules and engineering of novel protein–protein interfaces.