| pubmed-article:9062194 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9062194 | lifeskim:mentions | umls-concept:C0063710 | lld:lifeskim |
| pubmed-article:9062194 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
| pubmed-article:9062194 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:9062194 | lifeskim:mentions | umls-concept:C0231491 | lld:lifeskim |
| pubmed-article:9062194 | lifeskim:mentions | umls-concept:C1513371 | lld:lifeskim |
| pubmed-article:9062194 | pubmed:issue | 6621 | lld:pubmed |
| pubmed-article:9062194 | pubmed:dateCreated | 1997-4-3 | lld:pubmed |
| pubmed-article:9062194 | pubmed:abstractText | Inflammation, regardless of whether it is provoked by infection or by tissue damage, starts with the activation of macrophages which initiate a cascade of inflammatory responses by producing the cytokines interleukin-1 (IL-1) and tumour necrosis factor-alpha (ref. 1). Three naturally occurring ligands for the IL-1 receptor (IL1R) exist: the agonists IL-1alpha and IL-1beta and the IL-1-receptor antagonist IL1RA (ref. 2). IL-1 is the only cytokine for which a naturally occurring antagonist is known. Here we describe the crystal structure at 2.7 A resolution of the soluble extracellular part of type-I IL1R complexed with IL1RA. The receptor consists of three immunoglobulin-like domains. Domains 1 and 2 are tightly linked, but domain three is completely separate and connected by a flexible linker. Residues of all three domains contact the antagonist and include the five critical IL1RA residues which were identified by site-directed mutagenesis. A region that is important for biological function in IL-1beta, the 'receptor trigger site' is not in direct contact with the receptor in the IL1RA complex. Modelling studies suggest that this IL-1beta trigger site might induce a movement of domain 3. | lld:pubmed |
| pubmed-article:9062194 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9062194 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9062194 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9062194 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9062194 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9062194 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9062194 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9062194 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9062194 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9062194 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9062194 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:9062194 | pubmed:issn | 0028-0836 | lld:pubmed |
| pubmed-article:9062194 | pubmed:author | pubmed-author:AkesonAA | lld:pubmed |
| pubmed-article:9062194 | pubmed:author | pubmed-author:TardifCC | lld:pubmed |
| pubmed-article:9062194 | pubmed:author | pubmed-author:YanofskySS | lld:pubmed |
| pubmed-article:9062194 | pubmed:author | pubmed-author:SoffientiniAA | lld:pubmed |
| pubmed-article:9062194 | pubmed:author | pubmed-author:BarrettR WRW | lld:pubmed |
| pubmed-article:9062194 | pubmed:author | pubmed-author:SchreuderHH | lld:pubmed |
| pubmed-article:9062194 | pubmed:author | pubmed-author:SarubbiEE | lld:pubmed |
| pubmed-article:9062194 | pubmed:author | pubmed-author:BowlinTT | lld:pubmed |
| pubmed-article:9062194 | pubmed:author | pubmed-author:Trump-Kallmey... | lld:pubmed |
| pubmed-article:9062194 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9062194 | pubmed:day | 13 | lld:pubmed |
| pubmed-article:9062194 | pubmed:volume | 386 | lld:pubmed |
| pubmed-article:9062194 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9062194 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9062194 | pubmed:pagination | 194-200 | lld:pubmed |
| pubmed-article:9062194 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:9062194 | pubmed:meshHeading | pubmed-meshheading:9062194-... | lld:pubmed |
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| pubmed-article:9062194 | pubmed:meshHeading | pubmed-meshheading:9062194-... | lld:pubmed |
| pubmed-article:9062194 | pubmed:meshHeading | pubmed-meshheading:9062194-... | lld:pubmed |
| pubmed-article:9062194 | pubmed:meshHeading | pubmed-meshheading:9062194-... | lld:pubmed |
| pubmed-article:9062194 | pubmed:meshHeading | pubmed-meshheading:9062194-... | lld:pubmed |
| pubmed-article:9062194 | pubmed:meshHeading | pubmed-meshheading:9062194-... | lld:pubmed |
| pubmed-article:9062194 | pubmed:meshHeading | pubmed-meshheading:9062194-... | lld:pubmed |
| pubmed-article:9062194 | pubmed:meshHeading | pubmed-meshheading:9062194-... | lld:pubmed |
| pubmed-article:9062194 | pubmed:meshHeading | pubmed-meshheading:9062194-... | lld:pubmed |
| pubmed-article:9062194 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9062194 | pubmed:articleTitle | A new cytokine-receptor binding mode revealed by the crystal structure of the IL-1 receptor with an antagonist. | lld:pubmed |
| pubmed-article:9062194 | pubmed:affiliation | Marion Merrell Dow Research Institute, Strasbourg, France. | lld:pubmed |
| pubmed-article:9062194 | pubmed:publicationType | Journal Article | lld:pubmed |
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