Crystal Structures of Two Human Vitronectin, Urokinase and Urokinase Receptor Complexes

Journal Article · Tue Jan 01 04:00:00 EST 2008 · Nature Structural and Molecular Biology

DOI:https://doi.org/10.1038/nsmb.1404· OSTI ID:959840

Huai, Q; Zhou, A; Lin, L; Mazar, A; parry, G; Callahan, J; Shaw, D; Furie, B; Furie, B; Huang, M

The urokinase receptor (uPAR) can recognize several ligands. The structural basis for this multiple ligand recognition by uPAR is unknown. This study reports the crystal structures of uPAR in complex with both urokinase (uPA) and vitronectin and reveal that uPA occupies the central cavity of the receptor, whereas vitronectin binds at the outer side of the receptor. These results provide a structural understanding of one receptor binding to two ligands.

• Research Organization: Brookhaven National Laboratory (BNL) National Synchrotron Light Source
• Sponsoring Organization: Doe - Office Of Science
• DOE Contract Number: AC02-98CH10886
• OSTI ID: 959840
• Report Number(s): BNL--82826-2009-JA
• Journal Information: Nature Structural and Molecular Biology, Journal Name: Nature Structural and Molecular Biology Journal Issue: 4 Vol. 15
• Country of Publication: United States
• Language: English

Related Subjects

36 MATERIALS SCIENCE
CRYSTAL STRUCTURE
LIGANDS
RECEPTORS
UROKINASE
national synchrotron light source