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

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Vis graf over relationer

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 (muPAR) is determined. The structure of DII and DIII of muPAR 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. This article is protected by copyright. All rights reserved.

OriginalsprogEngelsk
TidsskriftFEBS Letters
Vol/bind593
Udgave nummer11
Sider (fra-til)1236-1247
Antal sider12
ISSN0014-5793
DOI
StatusUdgivet - 1 jun. 2019

Bibliografisk note

This article is protected by copyright. All rights reserved.

ID: 57150248