Chaperone-assisted structure elucidation with DARPins. (February 2020)

• Record Type: Journal Article
• Authors: Mittl, Peer RE; Ernst, Patrick; Plückthun, Andreas
• Is Part Of: Current opinion in structural biology. Volume 60(2020)
• Page Start: 93
• Page End: 100
• Publication Date: 2020-02
• Subjects: Molecular biology -- Periodicals; 570
• DOI: 10.1016/j.sbi.2019.12.009
• Languages: English
• ISSNs: 0959-440X

Abstract

Abstract : Designed ankyrin repeat proteins (DARPins) are artificial binding proteins that have found many uses in therapy, diagnostics and biochemical research. They substantially extend the scope of antibody-derived binders. Their high affinity and specificity, rigidity, extended paratope, and facile bacterial production make them attractive for structural biology. Complexes with simple DARPins have been crystallized for a long time, but particularly the rigid helix fusion strategy has opened new opportunities. Rigid DARPin fusions expand crystallization space, enable recruitment of targets in a host lattice and reduce the size limit for cryo-EM. Besides applications in structural biology, rigid DARPin fusions also serve as molecular probes in cells to investigate spatial restraints in targets.