Chaperone-assisted structure elucidation with DARPins

被引:19
|
作者
Mittl, Peer R. E. [1 ]
Ernst, Patrick [1 ]
Plueckthun, Andreas [1 ]
机构
[1] Univ Zurich, Dept Biochem, Winterthurerstr 190, CH-8057 Zurich, Switzerland
关键词
ANKYRIN REPEAT PROTEINS; BINDING-PROTEINS; CRYSTALLIZATION; DESIGN; SPECIFICITY; FACILITATE; INHIBITORS; LIBRARIES; SELECTION; BINDERS;
D O I
10.1016/j.sbi.2019.12.009
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:93 / 100
页数:8
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