Linked Life Data

18508598

Source:http://linkedlifedata.com/resource/pubmed/id/18508598

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2008-5-29
pubmed:abstractText
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1093-4715
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
13
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
5441-61
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Structure and ligand interactions of the urokinase receptor (uPAR).
pubmed:affiliation
Finsen Laboratory, Rigshospitalet section 3735, Copenhagen Biocenter room 3.3.31, Ole Maaloes Vej 5, DK-2200 Copenhagen N, Denmark.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't