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

Riittinen, L.; Limongi, P.; Crippa, M.P.; Conese, M.; Hernandez-Marrero, L.; Fazioli, F.; Blasi, F.

FEBS Letters 381(1-2): 1-6


ISSN/ISBN: 0014-5793
PMID: 8641412
DOI: 10.1016/0014-5793(96)00033-6
Accession: 009335845

Download citation:  

Article/Abstract emailed within 0-6 h
Payments are secure & encrypted
Powered by Stripe
Powered by PayPal

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.