Removal of domain D2 or D3 of the human urokinase receptor does not affect ligand affinity

Abstract
The main ligand‐binding determinant of the human urokinase receptor (uPAR) is located in the amino terminal domain D1, but when isolated this domain presents a 1500 fold lower affinity than the intact three‐domain uPAR (D1D2D3) [1]. uPAR mutants missing either domain 2 (D1HD3) or domain 3 (D1D2) were expressed in murine LB6 cells and showed to be properly GPI‐anchored to the cell surface. Binding assays with [125I]ATF demonstrated that these mutants possessed a normal (D1D2) or slightly reduced (D1HD3) affinity, indicating that a high ligand‐affinity may be achieved by a combination of D1 with domain D2 or D3.

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