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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 Regan
The 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

Structure

ISSN

0969-2126

Publisher

Cell Press

Issue

5

Volume

11

Page range

497-508

Pages

12.0

Department 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

2012-02-06

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