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  • Title: Computational design of a symmetric homodimer using β-strand assembly.
    Author: Stranges PB, Machius M, Miley MJ, Tripathy A, Kuhlman B.
    Journal: Proc Natl Acad Sci U S A; 2011 Dec 20; 108(51):20562-7. PubMed ID: 22143762.
    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.
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