IMR Press / FBL / Volume 13 / Issue 14 / DOI: 10.2741/3092

Frontiers in Bioscience-Landmark (FBL) is published by IMR Press from Volume 26 Issue 5 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on as a courtesy and upon agreement with Frontiers in Bioscience.

Open Access Article
Structure and ligand interactions of the urokinase receptor (uPAR)
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1 Finsen Laboratory, Rigshospitalet section 3735, Copenhagen Biocenter room 3.3.31, Ole Maaloes Vej 5, DK-2200 Copenhagen N, Denmark
2 SBiN-Lab, Department of Biology, University of Copenhagen, Copenhagen Biocenter room 3.0.41, Ole Maaloes Vej 5, DK-2200 Copenhagen N, Denmark
3 DrugMode Aps, Forskerparken 10C, DK-5230 Odense M., Denmark
Academic Editor:Pia Ragno
Front. Biosci. (Landmark Ed) 2008, 13(14), 5441–5461;
Published: 1 May 2008
(This article belongs to the Special Issue Urokinase-mediated plasminogen activation system)

The urokinase-type plasminogen activator receptor (uPAR or CD87) is a glycolipid-anchored membrane glycoprotein, which is responsible for focalizing plasminogen activation to the cell surface through its high-affinity binding to the serine protease uPA. This tight interaction (KD less than 1 nM) is accomplished by an unusually large and hydrophobic binding cavity in uPAR that is created by a unique interdomain assembly involving all three homologous domains of the receptor. These domains belong to the Ly-6/uPAR (LU) protein domain family, which is defined by a consensus sequence predominantly based on disulfide connectivities, and they adopt a characteristic three-finger fold. Interestingly, the gene for uPAR is localized in a cluster of 6 homologous genes encoding proteins with multiple LU-domains. The structural biology of uPAR will be reviewed with special emphasis on its multidomain composition and the interaction with its natural protein ligands, i.e. the serine protease uPA and the matrix protein vitronectin.

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