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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1992-2-18
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pubmed:abstractText |
Interleukin 1 (IL-1) is a family of polypeptide cytokines that plays an essential role in modulating immune and inflammatory responses. IL-1 activity is mediated by either of two distinct proteins, IL-1 alpha or IL-1 beta, both of which bind to the same receptor found on T-lymphocytes, fibroblasts and endothelial cells (Type 1 receptor). The effect of specific chemical modification of recombinant IL-1 alpha and IL-1 beta on receptor binding was examined. Modification of the proteins with phenylglyoxal, an arginine-specific reagent, resulted in the loss of Type 1 IL-1 receptor binding activity. The stoichiometry of this modification revealed that a single arginine in either IL-1 alpha or IL-1 beta is responsible for the loss of activity. Cyanogen bromide cleavage of phenylglyoxal modified IL-1 alpha and IL-1 beta, followed by sequencing of the peptides, revealed that arginine-12 in IL-1 alpha and arginine-4 in IL-1 beta, which occupy the same topology in the respective crystallographic structures, are the target of phenylglyoxal. These results suggest that an arginine residue plays an important role in ligand-receptor interaction.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Arginine,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-1,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Phenylglyoxal,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Immunologic,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Interleukin-1,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0006-3002
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
11
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pubmed:volume |
1118
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
25-35
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:1837236-Amino Acid Sequence,
pubmed-meshheading:1837236-Animals,
pubmed-meshheading:1837236-Arginine,
pubmed-meshheading:1837236-Crystallography,
pubmed-meshheading:1837236-Humans,
pubmed-meshheading:1837236-Interleukin-1,
pubmed-meshheading:1837236-Magnetic Resonance Spectroscopy,
pubmed-meshheading:1837236-Mice,
pubmed-meshheading:1837236-Molecular Sequence Data,
pubmed-meshheading:1837236-Peptide Fragments,
pubmed-meshheading:1837236-Phenylglyoxal,
pubmed-meshheading:1837236-Protein Binding,
pubmed-meshheading:1837236-Protein Conformation,
pubmed-meshheading:1837236-Receptors, Immunologic,
pubmed-meshheading:1837236-Receptors, Interleukin-1,
pubmed-meshheading:1837236-Recombinant Proteins
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pubmed:year |
1991
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pubmed:articleTitle |
The role of arginine residues in interleukin 1 receptor binding.
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pubmed:affiliation |
Department of Protein Biochemistry, Roche Research Center, Hoffmann-La Roche Inc., Nutley, NJ 07110-1199.
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pubmed:publicationType |
Journal Article,
In Vitro
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