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PEDS Advance Access originally published online on May 27, 2004
Protein Engineering Design and Selection 2004 17(4):399-409; doi:10.1093/protein/gzh047
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Protein Engineering, Design & Selection vol. 17 no. 4 © Oxford University Press 2004; all rights reserved

Protein design to understand peptide ligand recognition by tetratricopeptide repeat proteins

Aitziber L. Cortajarena1, Tommi Kajander1, Weilan Pan1, Melanie J. Cocco1,2 and Lynne Regan1,3,4

1Department of Molecular Biophysics and Biochemistry and 3Department of Chemistry, Yale University, PO Box 208114, New Haven, CT 06520-8114, USA 2Present address: Department of Molecular Biology and Biochemistry, University of California, 1218 Natural Sciences I, Irvine, CA 92697-3900 USA

4 To whom correspondence should be addressed. E-mail: lynne.regan{at}yale.edu

Protein design aims to understand the fundamentals of protein structure by creating novel proteins with pre-specified folds. An equally important goal is to understand protein function by creating novel proteins with pre-specified activities. Here we describe the design and characterization of a tetratricopeptide (TPR) protein, which binds to the C-terminal peptide of the eukaryotic chaperone Hsp90. The design emphasizes the importance of both direct, short-range protein–peptide interactions and of long-range electrostatic optimization. We demonstrate that the designed protein binds specifically to the desired peptide and discriminates between it and the similar C-terminal peptide of Hsp70.

Received May 11, 2004; accepted May 17, 2004.

Edited by Alan Fersht


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