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Structural Basis for Simvastatin Competitive Antagonism of Complement Receptor 3.

J Biol Chem. 2016; 
Jensen MR, Bajic G, Zhang X, Laustsen AK, Koldsø H, Skeby KK, Schiøtt B, Andersen GR, Vorup-Jensen T.
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摘要

The complement system is an important part of the innate immune response to infection but may also cause severe complications during inflammation. Small molecule antagonists to complement receptor 3 (CR3) have been widely sought, but a structural basis for their mode of action is not available. We report here on the structure of the human CR3 ligand-binding I domain in complex with simvastatin. Simvastatin targets the metal ion-dependent adhesion site of the open, ligand-binding conformation of the CR3 I domain by direct contact with the chelated Mg(2+) ion. Simvastatin antagonizes I domain binding to the complement fragments iC3b and C3d but not to intercellular adhesion molecule-1. By virtue of the I domain's... More

关键词

anti-inflammatory therapy; cell adhesion; complement; inflammation; integrin; molecular dynamics; protein drug interaction; receptor structure-function; statin; surface plasmon resonance (SPR)