Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3
|
| pubmed:dateCreated |
1997-5-28
|
| pubmed:abstractText |
The extracellular domain of the type I Interleukin-1 receptor (sIL-1R) was expressed in Drosophila S2 cells as a secreted 43 kDa glycoprotein, as evidenced by its binding to Concanavalin A and enzymatic deglycosylation. sIL-1R bound IL-1 beta with a K(D) of 2 nM as determined by competition ELISA. N-Glycanase treated sIL-1R had a C. 100 fold lower affinity than glycosylated sIL-1R for IL-1 beta, suggesting that glycosylation is a key component of the IL-1 beta/IL-1 receptor interaction. Crosslinking of sIL-1R to (125)I-IL-1 beta could be competed with unlabelled IL-1 alpha, IL-1 beta, IL-1 receptor antagonist (IL-1ra), and a mutant of IL-1 (Th9Gly) which has reduced bioactivity but wild type receptor binding affinity. Limited proteolysis of sIL-1R in the presence of IL-1 alpha, IL-1 beta, IL-1ra, and Thr9Gly IL-1 beta with several different proteases followed by analysis of sIL-1R by Western blot was used to assess the effect of binding on sIL-1R conformation. While some proteases showed no differences in cleavage patterns or sensitivity between free and bound sIL-1R, others showed differences in either cleavage sites or sensitivity with different ligands. This implies that upon ligand binding there is a conformational change in the receptor which is sensitive to the particular ligand bound, and hence has implications for the ability of different ligands to trigger responses after binding to receptor.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cross-Linking Reagents,
http://linkedlifedata.com/resource/pubmed/chemical/Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-1,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Interleukin-1,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Interleukin-1 Type I,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Mar
|
| pubmed:issn |
1043-4666
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
8
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
206-13
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:8833035-Animals,
pubmed-meshheading:8833035-Binding Sites,
pubmed-meshheading:8833035-Cell Line,
pubmed-meshheading:8833035-Cloning, Molecular,
pubmed-meshheading:8833035-Cross-Linking Reagents,
pubmed-meshheading:8833035-Drosophila melanogaster,
pubmed-meshheading:8833035-Endopeptidases,
pubmed-meshheading:8833035-Glycosylation,
pubmed-meshheading:8833035-Humans,
pubmed-meshheading:8833035-Interleukin-1,
pubmed-meshheading:8833035-Ligands,
pubmed-meshheading:8833035-Liver,
pubmed-meshheading:8833035-Protein Conformation,
pubmed-meshheading:8833035-Receptors, Interleukin-1,
pubmed-meshheading:8833035-Receptors, Interleukin-1 Type I,
pubmed-meshheading:8833035-Recombinant Fusion Proteins,
pubmed-meshheading:8833035-Substrate Specificity,
pubmed-meshheading:8833035-Transfection
|
| pubmed:year |
1996
|
| pubmed:articleTitle |
Type I IL-1 receptor: ligand specific confirmation differences and the role of glycosylation in ligand binding.
|
| pubmed:affiliation |
Department of Molecular Immunology, SmithKline Beecham Pharmaceuticals, King of Prussia, Pennsylvania, USA.
|
| pubmed:publicationType |
Journal Article
|