Crystal structure of the unoccupied murine urokinase‐type plasminogen activator receptor (uPAR) reveals a tightly packed DII–DIII unit

Author:

Liu Min12,Lin Lin3,Høyer‐Hansen Gunilla45,Ploug Michael45ORCID,Li Hanlin6,Jiang Longguang6ORCID,Yuan Cai1ORCID,Li Jinyu6,Huang Mingdong6

Affiliation:

1. College of Biological Science and Engineering Fuzhou University China

2. College of Life Science Fujian Normal University Fuzhou China

3. Beth Israel Deaconess Medical Center Harvard Medical School Boston MA USA

4. Biotechnology Research Innovation Centre (BRIC) University of Copenhagen Denmark

5. Finsen Laboratory Rigshospitalet Copenhagen Denmark

6. College of Chemistry Fuzhou University China

Funder

National Natural Science Foundation of China

Natural Science Foundation of Fujian Province

Publisher

Wiley

Subject

Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics

Reference78 articles.

1. Structure and ligand interactions of the urokinase receptor (uPAR);Kjaergaard M;Front Biosci,2008

2. Did evolution create a flexible ligand‐binding cavity in the urokinase receptor through deletion of a plesiotypic disulfide bond?;Leth JM;J Biol Chem,2019

3. Conserved structural determinants in three‐fingered protein domains;Galat A;FEBS J,2008

4. Cellular receptor for urokinase plasminogen‐activator – carboxyl‐terminal processing and membrane anchoring by glycosyl‐phosphatidylinositol;Ploug M;J Biol Chem,1991

5. Selective abrogation of the uPA‐uPAR interaction in vivo reveals a novel role in suppression of fibrin‐associated inflammation;Connolly BM;Blood,2010

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