Editor's Summary
22 September 2005
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.
News and Views: Structural biology: Form and function instructions
How much and what kind of information is required to fold a chain of amino acids into a functioning protein? It seems the problem may not be as daunting as once thought — the solution is in the coevolution data.
Jeffery W. Kelly
doi: 10.1038/437486a
Article: Evolutionary information for specifying a protein fold
Michael Socolich, Steve W. Lockless, William P. Russ, Heather Lee, Kevin H. Gardner and Rama Ranganathan
doi: 10.1038/nature03991
Abstract | Full Text | PDF (544K) | Supplementary information
Letter: Natural-like function in artificial WW domains
William P. Russ, Drew M. Lowery, Prashant Mishra, Michael B. Yaffe and Rama Ranganathan
doi: 10.1038/nature03990
First paragraph | Full Text | PDF (979K) | Supplementary information
