In April 2006, the crystal structure of suPAR was published in Science. The three-domain structure was shown to be able to differentially rotate around its main axis to accommodate a number of complex ligands1.
Due to this ability to change conformation, suPAR demonstrates a highly variable binding pocket, which is believed to explain its immense value in a number of different functions including cell signaling, cell migration, and immune response.
Amongst other functions, the receptor for urokinase plasminogen activator (uPAR) promotes invasion by neoplastic or inflammatory cells by focusing proteolysis of urokinase to the cell surface. In pathologic conditions, soluble forms of the receptor (suPAR) are released and activate cell receptors to promote chemotaxis and immune response.