The de novo design of protein-binding peptides is challenging because it requires the identification of both a sequence and a backbone conformation favorable for binding. We used a computational strategy that iterates between structure and sequence optimization to redesign the C-terminal portion of the RGS14 GoLoco motif peptide so that it adopts a new conformation when bound to Gαi1. An X-ray crystal structure of the redesigned complex closely matches the computational model, with a backbone root-mean-square deviation of 1.1 Å.
|Original language||English (US)|
|Number of pages||3|
|Journal||Journal of the American Chemical Society|
|State||Published - Mar 30 2011|
ASJC Scopus subject areas
- Colloid and Surface Chemistry