Crystallization of soluble urokinase receptor (suPAR) in complex with urokinase amino-terminal fragment (1–143)
✍ Scribed by Huang, Mingdong ;Mazar, Andrew P. ;Parry, Graham ;Higazi, Abd Al-Roof ;Kuo, Alice ;Cines, Douglas B.
- Book ID
- 104478107
- Publisher
- International Union of Crystallography
- Year
- 2005
- Tongue
- English
- Weight
- 230 KB
- Volume
- 61
- Category
- Article
- ISSN
- 0907-4449
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✦ Synopsis
Urokinase-type plasminogen activator (urokinase, uPA) and its receptor, uPAR, have been implicated in cell adhesion, migration, tissue remodelling and tumour-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 Å using a synchrotron X-ray source.