Crystal structures of two human vitronectin, urokinase and urokinase receptor complexes
Copyright policy )Crystal structures of two human vitronectin, urokinase and urokinase receptor complexes
The urokinase receptor (uPAR) can recognize several ligands. The structural basis for this multiple ligand recognition by uPAR is unknown. This study reports the crystal structures of uPAR in complex with both urokinase (uPA) and vitronectin and reveal that uPA occupies the central cavity of the receptor, whereas vitronectin binds at the outer side of the receptor. These results provide a structural understanding of one receptor binding to two ligands.
- University of Cambridge United Kingdom
- Wellcome Trust United Kingdom
- Beth Israel Deaconess Medical Center United States
- D. E. Shaw Research United States
Models, Molecular, Protein Conformation, Humans, Receptors, Cell Surface, Vitronectin, Crystallography, X-Ray, Urokinase-Type Plasminogen Activator, Protein Binding, Receptors, Urokinase Plasminogen Activator
Models, Molecular, Protein Conformation, Humans, Receptors, Cell Surface, Vitronectin, Crystallography, X-Ray, Urokinase-Type Plasminogen Activator, Protein Binding, Receptors, Urokinase Plasminogen Activator
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