Unknown

Dataset Information

0

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


ABSTRACT: 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.

SUBMITTER: Huai Q 

PROVIDER: S-EPMC2443823 | biostudies-literature | 2008 Apr

REPOSITORIES: biostudies-literature

altmetric image

Publications

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

Huai Qing Q   Zhou Aiwu A   Lin Lin L   Mazar Andrew P AP   Parry Graham C GC   Callahan Jennifer J   Shaw David E DE   Furie Bruce B   Furie Barbara C BC   Huang Mingdong M  

Nature structural & molecular biology 20080323 4


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. ...[more]

Similar Datasets

| S-EPMC5120694 | biostudies-literature
| S-EPMC5730292 | biostudies-literature
| S-EPMC3172387 | biostudies-literature
| S-EPMC5615192 | biostudies-literature
| S-EPMC5418785 | biostudies-literature
| S-EPMC1142576 | biostudies-literature
| S-EPMC5382625 | biostudies-literature
| S-EPMC2144633 | biostudies-other
| S-EPMC3258879 | biostudies-other
| S-EPMC9064986 | biostudies-literature