Design of stable alpha-helical arrays from an idealized TPR motif

Main, Ewan R G, Xiong, Yong, Cocco, Melanie J, D'Andrea, Luca and Regan, Lynne (2003) Design of stable alpha-helical arrays from an idealized TPR motif. Structure, 11 (5). pp. 497-508. ISSN 0969-2126

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Abstract

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.

Item Type: Article
Additional Information: 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.
Schools and Departments: School of Life Sciences > Chemistry
Depositing User: Ewan Main
Date Deposited: 06 Feb 2012 20:13
Last Modified: 30 Nov 2012 17:06
URI: http://sro.sussex.ac.uk/id/eprint/24753
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