Computational design of the sequence and structure of a protein-binding peptide.

ABSTRACT: 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 G?(i1). 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.

SUBMITTER: Sammond DW 

PROVIDER: S-EPMC3081598 | biostudies-literature | 2011 Mar

REPOSITORIES: biostudies-literature