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 urokina se-type plasminogen activator (uPA) and its specific glycolipid-anchor ed cell surface receptor (uPAR). uPAR is composed of three homologous domains and is the only multi-domain member of the Ly-6 family of glyc olipid-anchored membrane proteins. Recent evidence has highlighted sim ilarities between the individual domains of uPAR and the large family of secreted, single domain snake venom alpha-neurotoxins, suggesting t hat uPAR may adopt the same gross folding pattern as these structurall y well characterized proteins. Structural aspects of the binding betwe en a-neurotoxins and the acetylcholine receptor may have a major influ ence on future studies of the interaction between uPA and uPAR.