Structure and ligand interactions of the urokinase receptor (uPAR)

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

  • Magnus Kjærgaard
  • Line V Hansen, Danmark
  • Benedikte Jacobsen, Afdeling III, Danmark
  • Henrik Gardsvoll
  • ,
  • Michael Ploug
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.
OriginalsprogEngelsk
TidsskriftFrontiers in Bioscience
Vol/bind13
Sider (fra-til)5441-61
Antal sider21
ISSN1093-9946
StatusUdgivet - 2008
Eksternt udgivetJa

Se relationer på Aarhus Universitet Citationsformater

ID: 70231295