This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1na0
From Proteopedia
Design of Stable alpha-Helical Arrays from an Idealized TPR Motif
Overview
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.
About this Structure
Full crystallographic information is available from OCA.
Reference
Design of stable alpha-helical arrays from an idealized TPR motif., Main ER, Xiong Y, Cocco MJ, D'Andrea L, Regan L, Structure. 2003 May;11(5):497-508. PMID:12737816 Page seeded by OCA on Sat May 3 02:16:48 2008
Categories: Andrea, L D. | Cocco, M. | Main, E. | Regan, L. | Xiong, Y. | Design | Tpr
