| pubmed-article:2001363 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2001363 | lifeskim:mentions | umls-concept:C0021753 | lld:lifeskim |
| pubmed-article:2001363 | lifeskim:mentions | umls-concept:C0037633 | lld:lifeskim |
| pubmed-article:2001363 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:2001363 | lifeskim:mentions | umls-concept:C0877853 | lld:lifeskim |
| pubmed-article:2001363 | lifeskim:mentions | umls-concept:C1382100 | lld:lifeskim |
| pubmed-article:2001363 | lifeskim:mentions | umls-concept:C0450363 | lld:lifeskim |
| pubmed-article:2001363 | pubmed:issue | 9 | lld:pubmed |
| pubmed-article:2001363 | pubmed:dateCreated | 1991-4-18 | lld:pubmed |
| pubmed-article:2001363 | pubmed:abstractText | The determination of the high-resolution three-dimensional solution structure of interleukin 1 beta (IL-1 beta), a protein of 153 residues and 17.4 kDa, which plays a central role in the immune and inflammatory responses, has been determined by heteronuclear (13C and 15N) three- and four-dimensional NMR spectroscopy. The structure is based on 3146 experimental restraints comprising 2780 distance and 366 torsion angle (phi, psi, and chi 1) restraints. A total of 32 simulated annealing structures are calculated, and the atomic RMS distribution about the mean coordinate positions is 0.41 +/- 0.04 A for the backbone atoms and 0.82 +/- 0.04 A for all atoms (excluding residue 1 at the N-terminus and residues 152 and 153 at the C-terminus, which are partially disordered). In the case of internal side chains with a surface accessibility of less than or equal to 40%, the atomic RMS distribution about the mean coordinate positions for all atoms is 0.49 +/- 0.03 A. IL-1 beta resembles a tetrahedron and is composed of 12 beta-strands arranged in three pseudosymmetric topological units, each of which comprises 5 strands. Analysis of the mutational data on IL-1 beta in the light of the three-dimensional structure suggests the presence of three distinct binding sites for the IL-1 receptor on the surface of the protein. It is suggested that each of the three immunoglobulin domains which comprise the extracellular portion of the IL-1 receptor recognizes one of these sites. | lld:pubmed |
| pubmed-article:2001363 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2001363 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2001363 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2001363 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2001363 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:2001363 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2001363 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2001363 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:2001363 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:2001363 | pubmed:author | pubmed-author:WingfieldP... | lld:pubmed |
| pubmed-article:2001363 | pubmed:author | pubmed-author:CloreG MGM | lld:pubmed |
| pubmed-article:2001363 | pubmed:author | pubmed-author:GronenbornA... | lld:pubmed |
| pubmed-article:2001363 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2001363 | pubmed:day | 5 | lld:pubmed |
| pubmed-article:2001363 | pubmed:volume | 30 | lld:pubmed |
| pubmed-article:2001363 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2001363 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2001363 | pubmed:pagination | 2315-23 | lld:pubmed |
| pubmed-article:2001363 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:2001363 | pubmed:meshHeading | pubmed-meshheading:2001363-... | lld:pubmed |
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| pubmed-article:2001363 | pubmed:meshHeading | pubmed-meshheading:2001363-... | lld:pubmed |
| pubmed-article:2001363 | pubmed:meshHeading | pubmed-meshheading:2001363-... | lld:pubmed |
| pubmed-article:2001363 | pubmed:meshHeading | pubmed-meshheading:2001363-... | lld:pubmed |
| pubmed-article:2001363 | pubmed:meshHeading | pubmed-meshheading:2001363-... | lld:pubmed |
| pubmed-article:2001363 | pubmed:meshHeading | pubmed-meshheading:2001363-... | lld:pubmed |
| pubmed-article:2001363 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:2001363 | pubmed:articleTitle | High-resolution three-dimensional structure of interleukin 1 beta in solution by three- and four-dimensional nuclear magnetic resonance spectroscopy. | lld:pubmed |
| pubmed-article:2001363 | pubmed:affiliation | Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892. | lld:pubmed |
| pubmed-article:2001363 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2001363 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| literatureCitation:1654_200... | literatureCitation:pubmed | pubmed-article:2001363 | lld:drugbank |
| entrez-gene:3553 | entrezgene:pubmed | pubmed-article:2001363 | lld:entrezgene |
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