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PEDS Advance Access published online on May 27, 2004
Protein Engineering Design and Selection, doi:10.1093/protein/gzh047
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Received May 11, 2004
Accepted May 17, 2004

Article

Protein design to understand peptide ligand recognition by tetratricopeptide repeat proteins

Aitziber L. Cortajarena 1, Tommi Kajander 1, Weilan Pan 1, Melanie J. Cocco 1, Lynne Regan 2*

1 Department of Molecular Biophysics & Biochemistry, Yale University, PO Box 208114, New Haven, CT 06520-8114
2 Department of Molecular Biophysics & Biochemistry, Yale University, PO Box 208114, New Haven, CT 06520-8114; Department of Chemistry, Yale University, New Haven, CT, USA

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


  Abstract

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.

Keywords: consensus sequence, electrostatics, Hsp90, protein design, tetratricopeptide repeat (TPR)


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