Crystal structures of two human vitronectin, urokinase and urokinase receptor complexes
- 23 March 2008
- journal article
- research article
- Published by Springer Nature in Nature Structural & Molecular Biology
- Vol. 15 (4) , 422-423
- https://doi.org/10.1038/nsmb.1404
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.Keywords
This publication has 11 references indexed in Scilit:
- uPAR-induced cell adhesion and migration: vitronectin provides the keyThe Journal of cell biology, 2007
- Mapping of the Vitronectin-binding Site on the Urokinase ReceptorJournal of Biological Chemistry, 2007
- Does the urokinase receptor exist in a latent form?Cellular and Molecular Life Sciences, 2007
- Structure of Human Urokinase Plasminogen Activator in Complex with Its ReceptorScience, 2006
- Crystal structure of the human urokinase plasminogen activator receptor bound to an antagonist peptideThe EMBO Journal, 2005
- How vitronectin binds PAI-1 to modulate fibrinolysis and cell migrationNature Structural & Molecular Biology, 2003
- uPAR: a versatile signalling orchestratorNature Reviews Molecular Cell Biology, 2002
- Urokinase Regulates Vitronectin Binding by Controlling Urokinase Receptor OligomerizationJournal of Biological Chemistry, 2002
- Structural and Functional Analysis of the Plasminogen Activator Inhibitor-1 Binding Motif in the Somatomedin B Domain of VitronectinPublished by Elsevier ,1996
- Serotonin 5-HT2a and 5-HT2c Receptors Stimulate Amyloid Precursor Protein Ectodomain SecretionJournal of Biological Chemistry, 1996