Premium
Removal of domain D2 or D3 of the human urokinase receptor does not affect ligand affinity
Author(s) -
Riittinen Leena,
Limongi Paola,
Crippa Massimo P.,
Conese Massimo,
Hernandez-Marrero Luciano,
Fazioli Francesca,
Blasi Francesco
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)00033-6
Subject(s) - urokinase receptor , mutant , receptor , ligand (biochemistry) , chemistry , microbiology and biotechnology , biophysics , biochemistry , biology , gene
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 [ 125 I]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.