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Proc Natl Acad Sci U S A. 2011 Dec 20;108(51):20562-7. doi: 10.1073/pnas.1115124108. Epub 2011 Dec 5.

Computational design of a symmetric homodimer using β-strand assembly.

Author information

  • 1Department of Biochemistry and Biophysics, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.

Abstract

Computational design of novel protein-protein interfaces is a test of our understanding of protein interactions and has the potential to allow modification of cellular physiology. Methods for designing high-affinity interactions that adopt a predetermined binding mode have proved elusive, suggesting the need for new strategies that simplify the design process. A solvent-exposed backbone on a β-strand is thought of as "sticky" and β-strand pairing stabilizes many naturally occurring protein complexes. Here, we computationally redesign a monomeric protein to form a symmetric homodimer by pairing exposed β-strands to form an intermolecular β-sheet. A crystal structure of the designed complex closely matches the computational model (rmsd = 1.0 Å). This work demonstrates that β-strand pairing can be used to computationally design new interactions with high accuracy.

PMID:
22143762
[PubMed - indexed for MEDLINE]
PMCID:
PMC3251150
Free PMC Article
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