| pubmed-article:2602367 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2602367 | lifeskim:mentions | umls-concept:C0021753 | lld:lifeskim |
| pubmed-article:2602367 | lifeskim:mentions | umls-concept:C2699488 | lld:lifeskim |
| pubmed-article:2602367 | pubmed:issue | 24 | lld:pubmed |
| pubmed-article:2602367 | pubmed:dateCreated | 1990-2-1 | lld:pubmed |
| pubmed-article:2602367 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2602367 | pubmed:abstractText | The structure of human recombinant interleukin 1 beta (IL-1 beta) has been refined by a restrained least-squares method to a crystallographic R factor of 17.2% to 2.0 A resolution. One-hundred sixty-eight solvent molecules have been located, and isotropic temperature factors for each atom have been refined. The overall structure is composed of 12 beta-strands that can best be described as forming the four triangular faces of a tetrahedron with hydrogen bonding resembling normal antiparallel beta-sheets only at the vertices. The interior of this tetrahedron is filled by hydrophobic side chains. Analysis of sequence alignments with IL-1 beta from other mammalian species shows the interior to be very well conserved with the exterior residues markedly less so. There does not appear to be a clustering of invariant amino acid side chains on the surface of the molecule, suggesting an area of interaction with the IL-1 receptor. Comparison of the IL-1 beta structure with IL-1 alpha sequences indicates that IL-1 alpha probably has a similar overall folding as IL-1 beta but binds to the receptor in a different fashion. The three-dimensional structure of the IL-1 beta is analyzed in light of what has been suggested by previously published work on mutants and fragments of the molecule. | lld:pubmed |
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| pubmed-article:2602367 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2602367 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2602367 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2602367 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2602367 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:2602367 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:2602367 | pubmed:author | pubmed-author:SchärH PHP | lld:pubmed |
| pubmed-article:2602367 | pubmed:author | pubmed-author:GrütterM GMG | lld:pubmed |
| pubmed-article:2602367 | pubmed:author | pubmed-author:PriestleJ PJP | lld:pubmed |
| pubmed-article:2602367 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2602367 | pubmed:volume | 86 | lld:pubmed |
| pubmed-article:2602367 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2602367 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2602367 | pubmed:pagination | 9667-71 | lld:pubmed |
| pubmed-article:2602367 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:2602367 | pubmed:year | 1989 | lld:pubmed |
| pubmed-article:2602367 | pubmed:articleTitle | Crystallographic refinement of interleukin 1 beta at 2.0 A resolution. | lld:pubmed |
| pubmed-article:2602367 | pubmed:affiliation | Pharmaceuticals Research Division, CIBA-Geigy Ltd., Basel, Switzerland. | lld:pubmed |
| pubmed-article:2602367 | pubmed:publicationType | Journal Article | lld:pubmed |
| entrez-gene:3553 | entrezgene:pubmed | pubmed-article:2602367 | lld:entrezgene |
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