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1na0
From Proteopedia
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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
1NA0 is a Protein complex structure of sequences from [1] with ACT, PB, CL, NA, MG and IPT as ligands. 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 [[Category: ]]
Page seeded by OCA on Sat Nov 24 22:48:37 2007
Categories: Protein complex | Andrea, L.D. | Cocco, M. | Main, E. | Regan, L. | Xiong, Y. | ACT | CL | IPT | MG | NA | PB | Design | Tpr
