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

Deanne W. Sammond, Dustin E. Bosch, Glenn L. Butterfoss, Carrie Purbeck, Mischa MacHius, David P. Siderovski, Brian Kuhlman

Research output: Contribution to journalArticle

37 Scopus citations

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 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 languageEnglish
Pages (from-to)4190-4192
Number of pages3
JournalJournal of the American Chemical Society
Volume133
Issue number12
DOIs
StatePublished - 30 Mar 2011

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    Sammond, D. W., Bosch, D. E., Butterfoss, G. L., Purbeck, C., MacHius, M., Siderovski, D. P., & Kuhlman, B. (2011). Computational design of the sequence and structure of a protein-binding peptide. Journal of the American Chemical Society, 133(12), 4190-4192. https://doi.org/10.1021/ja110296z