Crystallization of soluble urokinase receptor (suPAR) in complex with urokinase amino-terminal fragment (1-143)

被引：23

作者：

Huang, MD ^{[1
]}

Mazar, AP

Parry, G

Higazi, AA

Kuo, A

Cines, DB

机构：

[1] Chinese Acad Sci, Fujian Inst Res Struct Matter, State Key Lab Struct Chem, Fujian 350002, Peoples R China

[2] Beth Israel Deaconess Med Ctr, Boston, MA 02460 USA

[3] Attenuon LLC, San Diego, CA 92121 USA

[4] Univ Penn, Med Ctr, Dept Pathol & Lab Med, Philadelphia, PA 19104 USA

[5] Hadassah Med Ctr, Dept Clin Biochem, IL-91120 Jerusalem, Israel

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 2005年 / 61卷

关键词：

D O I：

10.1107/S0907444905014174

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

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 angstrom using a synchrotron X-ray source.

引用

页码：697 / 700

页数：4

共 35 条

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