Crystal structures of two human vitronectin, urokinase and urokinase receptor complexes

Qing Huai,Aiwu Zhou,Lin Lin,Andrew P Mazar,Graham C Parry,Jennifer Callahan,David E Shaw,Bruce Furie,Barbara C Furie,Mingdong Huang

NATURE STRUCTURAL & MOLECULAR BIOLOGY（2008）

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摘要

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.

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关键词

mechanism,cell biology,chromatin structure,vitronectin,protein binding,protein folding,receptors,receptor binding,rna,rna processing,dna recombination,signal transduction,gene expression,rnai,macromolecules,protein conformation,proteins,translation,chromatin,chromatin remodeling,transcription,crystal structure,biophysics,immune system,genetics,dna replication,apoptosis,ligands,dna repair,molecular,biochemistry,nucleic acids,molecular biology,cell cycle

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