Abstract
Binding of the urokinase plasminogen activator (uPA) to its cellular receptor (uPAR) mediates biological activities that play a role in tumor progression and metastasis. Huai et al. have determined the crystal structure of uPAR complexed with the amino-terminal receptor-binding fragment of uPA and an antibody to the receptor at 1.9 angstrom resolution. The receptor displays some conformational flexibility that may allow it to interact with a variety of ligands. The structure provides a basis for the design of uPA-uPAR antagonists. Q. Huai, A. P. Mazar, A. Kuo, G. C. Parry, D. E. Shaw, J. Callahan, Y. Li, C. Yuan, C. Bian, L. Chen, B. Furie, B. C. Furie, D. B. Cines, M. Huang, Structure of human urokinase plasminogen activator in complex with its receptor. Science 311 , 656-659 (2006). [Abstract] [Full Text]
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