Natural-like function in artificial WW domains

William P. Russ, Drew M. Lowery, Prashant Mishra, Michael B. Yaffe and Rama Ranganathan ()
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William P. Russ: University of Texas Southwestern Medical Center
Drew M. Lowery: Massachusetts Institute of Technology
Prashant Mishra: University of Texas Southwestern Medical Center
Michael B. Yaffe: Massachusetts Institute of Technology
Rama Ranganathan: University of Texas Southwestern Medical Center

Nature, 2005, vol. 437, issue 7058, 579-583

Abstract: Follow the sequence It is widely believed that a protein's amino acid sequence contains all the information needed to dictate its structure, but exactly what information is both necessary and sufficient for generating a folded, functional protein is not clear. Two papers by Rama Ranganathan and co-workers tackle this question using computational protein design to construct artificial WW domains, small proteins of approximately 40 amino acid residues that bind to proline-rich sequences. The synthetic proteins adopt the characteristic WW structure and recognize typical WW target sequences. Since the information used in designing these proteins was obtained from multiple sequence alignments only, with no prior knowledge of three-dimensional structure, it is clear that for some proteins, a relatively small quantity of sequence information is sufficient to specify the complex amino acid interactions that make up a functional protein.

Date: 2005
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DOI: 10.1038/nature03990

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