Crystallization of Soluble Urokinase Receptor (suPAR) in Complex with Urokinase Amino-Terminal Fragment (1-431)
Urokinase-type plasminogen activator (urokinase, uPA) and its receptor, uPAR, have been implicated in cell adhesion, migration, tissue remodeling and tumor-cell invasion. uPAR has three domains and is anchored to membranes by a glycosyl-phosphatidylinositol (GPI) anchor. Recombinant uPAR without its GPI anchor, soluble uPAR (suPAR), tends to oligomerize, making it difficult to crystallize. The amino-terminal fragment (ATF) of uPA is the major receptor-binding determinant in suPAR and binds to suPAR with nanomolar affinity, indistinguishable from membrane-bound uPAR. It is shown that uPA is capable of dissociating the oligomerization of suPAR and the crystallization of the suPAR-ATF complex is reported here. The resulting crystals diffract to 3.1 Angstroms using a synchrotron X-ray source.
- Research Organization:
- Brookhaven National Laboratory (BNL) National Synchrotron Light Source
- Sponsoring Organization:
- Doe - Office Of Science
- DOE Contract Number:
- AC02-98CH10886
- OSTI ID:
- 913866
- Report Number(s):
- BNL--78434-2007-JA
- Journal Information:
- Acta Cryst. D, Journal Name: Acta Cryst. D Journal Issue: 6 Vol. D61
- Country of Publication:
- United States
- Language:
- English
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