1NA3
Design of Stable alpha-Helical Arrays from an Idealized TPR Motif
Summary for 1NA3
| Entry DOI | 10.2210/pdb1na3/pdb |
| Related | 1NA0 |
| Descriptor | designed protein CTPR2, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, 1-methylethyl 1-thio-beta-D-galactopyranoside, ... (5 entities in total) |
| Functional Keywords | design, tpr, de novo protein |
| Biological source | unidentified |
| Total number of polymer chains | 2 |
| Total formula weight | 21351.33 |
| 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 Cited by 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: 12737816DOI: 10.1016/S0969-2126(03)00076-5 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.55 Å) |
Structure validation
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