1NA0

Design of Stable alpha-Helical Arrays from an Idealized TPR Motif

Summary for 1NA0

• Entry DOI: 10.2210/pdb1na0/pdb
• Related: 1NA3
• Descriptor: designed protein CTPR3, LEAD (II) ION, ACETATE ION, ... (8 entities in total)
• Functional Keywords: design, tpr, de novo protein
• Biological source: unidentified
• Total number of polymer chains: 2
• Total formula weight: 30415.84

Authors

Main, E.,Xiong, Y.,Cocco, M.,D'Andrea, L.,Regan, L. (deposition date: 2002-11-26, release date: 2003-06-03, Last modification date: 2024-02-14)

Primary citation

Main, E.,Xiong, Y.,Cocco, M.,D'Andrea, L.,Regan, L.
Design of Stable alpha-Helical Arrays from an Idealized TPR Motif
Structure, 11:497-508, 2003

PubMed 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.

PubMed: 12737816
DOI: 10.1016/S0969-2126(03)00076-5

Experimental method

X-RAY DIFFRACTION (1.6 Å)