A nanobody toolbox targeting dimeric coiled-coil modules for functionalization of designed protein origami structures

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Abstract
Significance: Coiled-coil dimers are structural motifs which occur frequently in natural proteins. They consist of two α-helices which wind around each other to form a supercoil and can be used as versatile modules for the construction of designed proteins. Here, nanobodies generated against the coiled-coil protein origami tetrahedral cage exhibit binding of one to four nanobodies per coiled-coil dimer in the tetrahedron and also in other types of protein origami structures. High-resolution structures of nanobodies bound to coiled-coil dimers revealed the range of binding motifs, including a positive allosteric binding to the tetrahedron and to the isolated coiled-coil dimeric module, introducing nanobodies as building modules in the protein assembly design.

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