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Structure of human urokinase plasminogen activator in complex with its receptor.

Authors
Type
Published Article
Journal
Science
1095-9203
Publisher
American Association for the Advancement of Science (AAAS)
Publication Date
Volume
311
Issue
5761
Pages
656–659
Identifiers
PMID: 16456079
Source
Medline

Abstract

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.

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