Study Reveals Process Linking Disordered Protein Folding and Binding

New Insights May Prove Useful In Future Protein Studies and Drug Development

LA JOLLA, CA, May 23, 2007—A group of scientists at The Scripps Research Institute and the Skaggs Institute for Chemical Biology have uncovered one of the processes by which disordered or unstructured proteins become bound to specific cellular sites. The findings offer valuable insights into how proteins carry out their genetically encoded functions, and may provide promising new targets for future drug development.

The study was published May 23, 2007 in an advance online edition of the journal Nature.

"Our study offers the first solid glimpse into the process that links folding and target site binding by an intrinsically unstructured protein," said Peter Wright, a Scripps Research scientist who led the research. "By applying advanced nuclear magnetic resonance (NMR) technology, we were able to show how disordered proteins recognize their targets and bind to them. As a result, we now know that the old dogma-that a defined protein structure equals protein function-is no longer the rule. A substantial number of proteins have large unstructured regions that are deeply involved in protein to protein interactions." .... continued