Structure and ligand interactions of the urokinase receptor (uPAR)

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Structure and ligand interactions of the urokinase receptor (uPAR). / Kjærgaard, Magnus; Hansen, Line V; Jacobsen, Benedikte; Gardsvoll, Henrik; Ploug, Michael.

I: Frontiers in Bioscience, Bind 13, 2008, s. 5441-61.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

Harvard

Kjærgaard, M, Hansen, LV, Jacobsen, B, Gardsvoll, H & Ploug, M 2008, 'Structure and ligand interactions of the urokinase receptor (uPAR)', Frontiers in Bioscience, bind 13, s. 5441-61.

APA

Kjærgaard, M., Hansen, L. V., Jacobsen, B., Gardsvoll, H., & Ploug, M. (2008). Structure and ligand interactions of the urokinase receptor (uPAR). Frontiers in Bioscience, 13, 5441-61.

CBE

Kjærgaard M, Hansen LV, Jacobsen B, Gardsvoll H, Ploug M. 2008. Structure and ligand interactions of the urokinase receptor (uPAR). Frontiers in Bioscience. 13:5441-61.

MLA

Vancouver

Kjærgaard M, Hansen LV, Jacobsen B, Gardsvoll H, Ploug M. Structure and ligand interactions of the urokinase receptor (uPAR). Frontiers in Bioscience. 2008;13:5441-61.

Author

Kjærgaard, Magnus ; Hansen, Line V ; Jacobsen, Benedikte ; Gardsvoll, Henrik ; Ploug, Michael. / Structure and ligand interactions of the urokinase receptor (uPAR). I: Frontiers in Bioscience. 2008 ; Bind 13. s. 5441-61.

Bibtex

@article{a06260dcb7f2476d897c9d5849a005a3,
title = "Structure and ligand interactions of the urokinase receptor (uPAR)",
abstract = "The urokinase-type plasminogen activator receptor (uPAR or CD87) is a glycolipid-anchored membrane glycoprotein, which is responsible for focalizing plasminogen activation to the cell surface through its high-affinity binding to the serine protease uPA. This tight interaction (KD less than 1 nM) is accomplished by an unusually large and hydrophobic binding cavity in uPAR that is created by a unique interdomain assembly involving all three homologous domains of the receptor. These domains belong to the Ly-6/uPAR (LU) protein domain family, which is defined by a consensus sequence predominantly based on disulfide connectivities, and they adopt a characteristic three-finger fold. Interestingly, the gene for uPAR is localized in a cluster of 6 homologous genes encoding proteins with multiple LU-domains. The structural biology of uPAR will be reviewed with special emphasis on its multidomain composition and the interaction with its natural protein ligands, i.e. the serine protease uPA and the matrix protein vitronectin.",
keywords = "Amino Acid Sequence, Cell Membrane, Conserved Sequence, Glycosylation, Hemoglobinuria, Paroxysmal, Humans, Ligands, Multigene Family, Protein Conformation, Protein Folding, Receptors, Cell Surface, Receptors, Urokinase Plasminogen Activator, Vitronectin",
author = "Magnus Kj{\ae}rgaard and Hansen, {Line V} and Benedikte Jacobsen and Henrik Gardsvoll and Michael Ploug",
year = "2008",
language = "English",
volume = "13",
pages = "5441--61",
journal = "Frontiers in Bioscience",
issn = "1093-9946",
publisher = "Frontiers in Bioscience",

}

RIS

TY - JOUR

T1 - Structure and ligand interactions of the urokinase receptor (uPAR)

AU - Kjærgaard, Magnus

AU - Hansen, Line V

AU - Jacobsen, Benedikte

AU - Gardsvoll, Henrik

AU - Ploug, Michael

PY - 2008

Y1 - 2008

N2 - The urokinase-type plasminogen activator receptor (uPAR or CD87) is a glycolipid-anchored membrane glycoprotein, which is responsible for focalizing plasminogen activation to the cell surface through its high-affinity binding to the serine protease uPA. This tight interaction (KD less than 1 nM) is accomplished by an unusually large and hydrophobic binding cavity in uPAR that is created by a unique interdomain assembly involving all three homologous domains of the receptor. These domains belong to the Ly-6/uPAR (LU) protein domain family, which is defined by a consensus sequence predominantly based on disulfide connectivities, and they adopt a characteristic three-finger fold. Interestingly, the gene for uPAR is localized in a cluster of 6 homologous genes encoding proteins with multiple LU-domains. The structural biology of uPAR will be reviewed with special emphasis on its multidomain composition and the interaction with its natural protein ligands, i.e. the serine protease uPA and the matrix protein vitronectin.

AB - The urokinase-type plasminogen activator receptor (uPAR or CD87) is a glycolipid-anchored membrane glycoprotein, which is responsible for focalizing plasminogen activation to the cell surface through its high-affinity binding to the serine protease uPA. This tight interaction (KD less than 1 nM) is accomplished by an unusually large and hydrophobic binding cavity in uPAR that is created by a unique interdomain assembly involving all three homologous domains of the receptor. These domains belong to the Ly-6/uPAR (LU) protein domain family, which is defined by a consensus sequence predominantly based on disulfide connectivities, and they adopt a characteristic three-finger fold. Interestingly, the gene for uPAR is localized in a cluster of 6 homologous genes encoding proteins with multiple LU-domains. The structural biology of uPAR will be reviewed with special emphasis on its multidomain composition and the interaction with its natural protein ligands, i.e. the serine protease uPA and the matrix protein vitronectin.

KW - Amino Acid Sequence

KW - Cell Membrane

KW - Conserved Sequence

KW - Glycosylation

KW - Hemoglobinuria, Paroxysmal

KW - Humans

KW - Ligands

KW - Multigene Family

KW - Protein Conformation

KW - Protein Folding

KW - Receptors, Cell Surface

KW - Receptors, Urokinase Plasminogen Activator

KW - Vitronectin

M3 - Journal article

C2 - 18508598

VL - 13

SP - 5441

EP - 5461

JO - Frontiers in Bioscience

JF - Frontiers in Bioscience

SN - 1093-9946

ER -