title: Crystal structures of two human vitronectin, urokinase and urokinase receptor complexes.
abstract: 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.
authors: Division of Hemostasis and Thrombosis, Beth Israel Deaconess Medical Center and Harvard Medical School, Boston, Massachusetts 02215, USA.
authors: Qing
authors: Q
authors: Huai
authors: Aiwu
authors: A
authors: Zhou
authors: Lin
authors: L
authors: Lin
authors: Andrew P
authors: AP
authors: Mazar
authors: Graham C
authors: GC
authors: Parry
authors: Jennifer
authors: J
authors: Callahan
authors: David E
authors: DE
authors: Shaw
authors: Bruce
authors: B
authors: Furie
authors: Barbara C
authors: BC
authors: Furie
authors: Mingdong
authors: M
authors: Huang
mesh_terms: D018360:Crystallography, X-Ray; D006801:Humans; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation; D011956:Receptors, Cell Surface / Q000737:chemistry / Q000378:metabolism*; D055293:Receptors, Urokinase Plasminogen Activator; D014568:Urokinase-Type Plasminogen Activator / Q000737:chemistry / Q000378:metabolism*; D019096:Vitronectin / Q000737:chemistry / Q000378:metabolism*
chemical_list: C524898:PLAUR protein, human; D011956:Receptors, Cell Surface; D055293:Receptors, Urokinase Plasminogen Activator; D019096:Vitronectin; D014568:Urokinase-Type Plasminogen Activator