The concave face of decorin mediates reversible dimerization and collagen binding

Abstract

Background: In the crystal structure of decorin, the concave faces of two monomers interact to form a tight dimer. Results: The decorin dimer in solution is in equilibrium with stable monomers, and mutations on the concave face abolish collagen binding. Conclusion: Decorin binds collagen as a monomer. Significance: These findings help resolve the controversy about the functional oligomeric state of decorin. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.