Structure-function relationships in the receptor for urokinase-type plasminogen activator. Comparison to other members of the Ly-6 family and snake venom alpha-neurotoxins.
Plasminogen activation is regulated by the interaction between urokinase-type plasminogen activator (uPA) and its specific glycolipid-anchored cell surface receptor (uPAR). uPAR is composed of three homologous domains and is the only multi-domain member of the Ly-6 family of glycolipid-anchored membrane proteins. Recent evidence has highlighted similarities between the individual domains of uPAR and the large family of secreted, single domain snake venom alpha-neurotoxins, suggesting that uPAR may adopt the same gross folding pattern as these structurally well characterized proteins. Structural aspects of the binding between alpha-neurotoxins and the acetylcholine receptor may have a major influence on future studies of the interaction between uPA and uPAR.
Ploug
M
M
Finsen Laboratory, Rigshospitalet, Copenhagen, Denmark.
Ellis
V
V
D000595:Amino Acid Sequence; D000818:Animals; D000950:Antigens, Ly / Q000235:genetics* / Q000378:metabolism; D008969:Molecular Sequence Data; D009498:Neurotoxins / Q000235:genetics*; D013329:Structure-Activity Relationship; D014568:Urokinase-Type Plasminogen Activator / Q000235:genetics* / Q000378:metabolism
D000950:Antigens, Ly; D009498:Neurotoxins; D014568:Urokinase-Type Plasminogen Activator