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Crystal structure of the unoccupied murine urokinase‐type plasminogen activator receptor ( uPAR ) reveals a tightly packed DII–DIII unit
Author(s) -
Liu Min,
Lin Lin,
HøyerHansen Gunilla,
Ploug Michael,
Li Hanlin,
Jiang Longguang,
Yuan Cai,
Li Jinyu,
Huang Mingdong
Publication year - 2019
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.13397
Subject(s) - urokinase receptor , vitronectin , plasminogen activator , chemistry , biophysics , receptor , urokinase , supar , microbiology and biotechnology , biochemistry , integrin , biology , endocrinology , genetics
The urokinase‐type plasminogen activator receptor ( uPAR ) is a cell surface receptor that is capable of binding to a range of extracellular proteins and triggering a series of proteolytic and signaling events. Previous structural studies of uPAR with its ligands uPA and vitronectin revealed that its three domains ( DI , DII , and DIII ) form a large hydrophobic cavity to accommodate uPA . In the present study, the structure of unoccupied murine uPAR (mu PAR ) is determined. The structure of DII and DIII of mu PAR is well defined and forms a compact globular unit, while DI could not be traced. Molecular dynamic simulations further confirm the rigid binding interface between DII and DIII . This study shows overall structural flexibility of uPAR in the absence of uPA .