Connecting two proteins using a fusion alpha helix stabilized by a chemical cross linker

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Building a sophisticated protein nano-assembly requires a method for linking protein components in a predictable and stable structure. Most of the cross linkers available have flexible spacers. Because of this, the linked hybrids have significant structural flexibility and the relative structure between their two components is largely unpredictable. Here we describe a method of connecting two proteins via a 'fusion a helix' formed by joining two pre-existing helices into a single extended helix. Because simple ligation of two helices does not guarantee the formation of a continuous helix, we used EY-CBS, a synthetic cross linker that has been shown to react selectively with cysteines in a-helices, to stabilize the connecting helix. Formation and stabilization of the fusion helix was confirmed by determining the crystal structures of the fusion proteins with and without bound EY-CBS. Our method should be widely applicable for linking protein building blocks to generate predictable structures.
Publisher
NATURE PUBLISHING GROUP
Issue Date
2016-05
Language
English
Article Type
Article
Citation

NATURE COMMUNICATIONS, v.7

ISSN
2041-1723
DOI
10.1038/ncomms11031
URI
http://hdl.handle.net/10203/208494
Appears in Collection
BS-Journal Papers(저널논문)CH-Journal Papers(저널논문)
Files in This Item
Nat Commun 2016, 7 11031.pdf(1.27 MB)Download
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