Structure of Human Urokinase Plasminogen Activator

Journal Article · Sun Jan 01 04:00:00 EST 2006 · Science

DOI:https://doi.org/10.1126/science.1121143· OSTI ID:914272

Huai, Q

The urokinase plasminogen activator binds to its cellular receptor with high affinity and initiates signaling cascades that are implicated in pathological processes including tumor growth, metastasis, and inflammation. We report the crystal structure at 1.9 angstroms of the urokinase receptor complexed with the urokinase amino-terminal fragment and an antibody against the receptor. The three domains of urokinase receptor form a concave shape with a central cone-shaped cavity where the urokinase fragment inserts. The structure provides insight into the flexibility of the urokinase receptor that enables its interaction with a wide variety of ligands and a basis for the design of urokinase-urokinase receptor antagonists.

• Research Organization: Brookhaven National Laboratory (BNL) National Synchrotron Light Source
• Sponsoring Organization: Doe - Office Of Science
• DOE Contract Number: AC02-98CH10886
• OSTI ID: 914272
• Report Number(s): BNL--78840-2007-JA
• Journal Information: Science, Journal Name: Science Vol. 311; ISSN 0193-4511; ISSN SCEHDK
• Country of Publication: United States
• Language: English

Related Subjects

36 MATERIALS SCIENCE
AFFINITY
CRYSTAL STRUCTURE
DESIGN
FLEXIBILITY
INFLAMMATION
NEOPLASMS
PLASMINOGEN
SHAPE
UROKINASE
national synchrotron light source