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

doi:10.1038/nsmb.1404

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^*

^*Corresponding author for this work

Pharmacology

Research output: Contribution to journal › Article › peer-review

101 Scopus citations

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.

Original language	English (US)
Pages (from-to)	422-423
Number of pages	2
Journal	Nature Structural and Molecular Biology
Volume	15
Issue number	4
DOIs	https://doi.org/10.1038/nsmb.1404
State	Published - Apr 2008

Funding

This research is supported by grants from the US National Institutes of Health (HL08658) and the American Heart Association (0330089N) (to M.H.) and from the British Heart Foundation (to A.Z.). Data for this study were measured at beam lines ID19 and ID24 of Advanced Photon Sources and at beam line X29 of the the National Synchrotron Light Source.

ASJC Scopus subject areas

Structural Biology
Molecular Biology

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10.1038/nsmb.1404

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title = "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.",

author = "Qing Huai and Aiwu Zhou and Lin Lin and Mazar, \{Andrew P.\} and Parry, \{Graham C.\} and Jennifer Callahan and Shaw, \{David E.\} and Bruce Furie and Furie, \{Barbara C.\} and Mingdong Huang",

note = "Funding Information: This research is supported by grants from the US National Institutes of Health (HL08658) and the American Heart Association (0330089N) (to M.H.) and from the British Heart Foundation (to A.Z.). Data for this study were measured at beam lines ID19 and ID24 of Advanced Photon Sources and at beam line X29 of the the National Synchrotron Light Source.",

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AU - Huai, Qing

AU - Zhou, Aiwu

AU - Lin, Lin

AU - Mazar, Andrew P.

AU - Parry, Graham C.

AU - Callahan, Jennifer

AU - Shaw, David E.

AU - Furie, Bruce

AU - Furie, Barbara C.

AU - Huang, Mingdong

N1 - Funding Information: This research is supported by grants from the US National Institutes of Health (HL08658) and the American Heart Association (0330089N) (to M.H.) and from the British Heart Foundation (to A.Z.). Data for this study were measured at beam lines ID19 and ID24 of Advanced Photon Sources and at beam line X29 of the the National Synchrotron Light Source.

PY - 2008/4

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N2 - 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.

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

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