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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
9
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pubmed:dateCreated |
1991-4-18
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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.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0006-2960
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
5
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pubmed:volume |
30
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2315-23
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:2001363-Amino Acid Sequence,
pubmed-meshheading:2001363-Calorimetry,
pubmed-meshheading:2001363-Carbon Isotopes,
pubmed-meshheading:2001363-Interleukin-1,
pubmed-meshheading:2001363-Magnetic Resonance Spectroscopy,
pubmed-meshheading:2001363-Models, Molecular,
pubmed-meshheading:2001363-Molecular Sequence Data,
pubmed-meshheading:2001363-Nitrogen Isotopes,
pubmed-meshheading:2001363-Protein Conformation,
pubmed-meshheading:2001363-Solutions
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pubmed:year |
1991
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pubmed:articleTitle |
High-resolution three-dimensional structure of interleukin 1 beta in solution by three- and four-dimensional nuclear magnetic resonance spectroscopy.
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pubmed:affiliation |
Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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