Linked Life Data

7498361

Source:http://linkedlifedata.com/resource/pubmed/id/7498361

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
13
pubmed:dateCreated
1996-1-16
pubmed:abstractText
The interaction of erythropoietin (Epo) with the erythropoietin receptor (EpoR) supports erythropoiesis. The EpoR is a member of the well-recognized cytokine receptor superfamily characterized by four conserved cysteines and a WSXWS domain in the extracellular portion of the molecule. To localize ligand-binding determinants of the EpoR near the WSXWS domain, we tested the ligand-binding ability of the wild-type human EpoR extracellular domain (EREx), two truncated and three chimeric constructs with the interleukin-2 receptor beta subunit (IL2R beta). Constructs were expressed in E. coli as GST fusion proteins linked to a solid-phase support and assayed for binding to 125I Epo. As previously shown, Epo bound specifically to the expressed extracellular domain, EREx. Epo did not bind to truncated receptors lacking either the entire fifth exon or the WSXWS domain. Epo also did not bind to chimeric receptors that had the amino acids encoded by the fifth exon replaced by IL2R beta or that had the amino acids subsequent to asparagine residue 209 replaced by IL2R beta. Specific binding was demonstrated for a construct in which the WSXWS was replaced by that of IL2R beta. We conclude that the amino acids encoded by this 5' portion of exon 5 of the EpoR are necessary for ligand binding and that the WSXWS domain is necessary for Epo binding but is not involved in ligand-binding specificity. We also speculate that if the putative soluble form of the EpoR is expressed (predicted to lack exon 5), it does not bind Epo and therefore may serve a physiologic purpose other than ligand binding.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0301-472X
pubmed:author
pubmed:issnType
Print
pubmed:volume
23
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1341-6
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Localization of an essential ligand binding determinant of the human erythropoietin receptor to a domain N-terminal to the WSXWS motif: implications for soluble receptor function.
pubmed:affiliation
University of Minnesota, Department of Pediatrics and Medicine, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't