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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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Liu, Min ; Lin, Lin ; Hansen, Gunilla Høyer ; Ploug, Michael ; Hanlin, Li ; Jiang, Longguang ; Yuan, Cai ; Li, Jinyu ; Huang, Mingdong. / Crystal structure of the unoccupied murine urokinase-type plasminogen activator receptor (uPAR) reveals a tightly packed DII-DIII unit. In: FEBS Letters. 2019 ; Vol. 593, No. 11. pp. 1236-1247.

Bibtex

@article{f15ef52d1bdd4c49be81ba4668e1b0a2,
title = "Crystal structure of the unoccupied murine urokinase-type plasminogen activator receptor (uPAR) reveals a tightly packed DII-DIII unit",
abstract = "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.",
keywords = "crystal structure, molecular dynamics, rigid, unoccupied, uPAR",
author = "Min Liu and Lin Lin and Hansen, {Gunilla H{\o}yer} and Michael Ploug and Li Hanlin and Longguang Jiang and Cai Yuan and Jinyu Li and Mingdong Huang",
note = "This article is protected by copyright. All rights reserved.",
year = "2019",
month = "6",
day = "1",
doi = "10.1002/1873-3468.13397",
language = "English",
volume = "593",
pages = "1236--1247",
journal = "FEBS Letters",
issn = "0014-5793",
publisher = "Elsevier BV",
number = "11",

}

RIS

TY - JOUR

T1 - Crystal structure of the unoccupied murine urokinase-type plasminogen activator receptor (uPAR) reveals a tightly packed DII-DIII unit

AU - Liu, Min

AU - Lin, Lin

AU - Hansen, Gunilla Høyer

AU - Ploug, Michael

AU - Hanlin, Li

AU - Jiang, Longguang

AU - Yuan, Cai

AU - Li, Jinyu

AU - Huang, Mingdong

N1 - This article is protected by copyright. All rights reserved.

PY - 2019/6/1

Y1 - 2019/6/1

N2 - 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.

AB - 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.

KW - crystal structure

KW - molecular dynamics

KW - rigid

KW - unoccupied

KW - uPAR

U2 - 10.1002/1873-3468.13397

DO - 10.1002/1873-3468.13397

M3 - Letter

VL - 593

SP - 1236

EP - 1247

JO - FEBS Letters

JF - FEBS Letters

SN - 0014-5793

IS - 11

ER -

ID: 57150248