Protein design to understand peptide ligand recognition by tetratricopeptide repeat proteins |
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Authors: | Cortajarena Aitziber L Kajander Tommi Pan Weilan Cocco Melanie J Regan Lynne |
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Affiliation: | Department of Molecular Biophysics and Biochemistry, Yale University, PO Box 208114, New Haven, CT 06520-8114, USA. |
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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. |
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Keywords: | consensus sequence/ electrostatics/ Hsp90/ protein design/ tetratricopeptide repeat |
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