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Design of stable alpha-helical arrays from an idealized TPR motif
journal contribution
posted on 2023-06-08, 05:28 authored by Ewan R G Main, Yong Xiong, Melanie J Cocco, Luca D'Andrea, Lynne ReganThe tetratricopeptide repeat (TPR) is a 34-amino acid alpha-helical motif that occurs in over 300 different proteins. In the different proteins, three to sixteen or more TPR motifs occur in tandem arrays and function to mediate protein-protein interactions. The binding specificity of each TPR protein is different, although the underlying structural motif is the same. Here we describe a statistical approach to the design of an idealized TPR motif. We present the high-resolution X-ray crystal structures (to 1.55 and 1.6 A) of designed TPR proteins and describe their solution properties and stability. A detailed analysis of these structures provides an understanding of the TPR motif, how it is repeated to give helical arrays with different superhelical twists, and how a very stable framework may be constructed for future functional designs.
History
Publication status
- Published
Journal
StructureISSN
0969-2126Publisher
Cell PressPublisher URL
External DOI
Issue
5Volume
11Page range
497-508Pages
12.0Department affiliated with
- Chemistry Publications
Notes
ERGM was first author (designed, performed, analyzed and wrote the majority of the work). One of the first of three successful designs for repeat proteins. The paper has been cited 34 times and has been presented at many international conferences.Full text available
- No
Peer reviewed?
- Yes
Legacy Posted Date
2012-02-06Usage metrics
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