Source:http://linkedlifedata.com/resource/pubmed/id/10880230
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
7
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pubmed:dateCreated |
2000-9-8
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pubmed:abstractText |
Previously, two binding sites for interleukin 5 (IL-5) were identified on the IL-5 receptor alpha chain (IL-5Ralpha). They are located within the CD loop of the first fibronectin type III (FnIII)-like domain and the EF loop of the second FnIII-like domain. The first binding site was identified by exploiting the different abilities of human IL-5Ralpha (hIL-5Ralpha) and mouse IL-5Ralpha (mIL-5Ralpha) to bind hIL-5. Here we show that ovine IL-5 (oIL-5) has the ability to activate the hIL-5Ralpha but not the mIL-5Ralpha. By using chimeras of the mIL-5Ralpha and hIL-5Ralpha we demonstrate that residues within the first and third FnIII-like domains of mIL-5Ralpha are responsible for this lack of activity. Furthermore, mutation of residues on hIL-5Ralpha to mIL-5Ralpha within the predicted DE and FG loop regions of the third FnIII domain reduces oIL-5 activity. These results show that regions of the third FnIII domain of IL-5Ralpha are involved in binding, in addition to the regions in domains one and two of the IL-5Ralpha that were identified in an earlier study.
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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 |
Jul
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pubmed:issn |
1043-4666
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pubmed:author | |
pubmed:copyrightInfo |
Copyright 2000 Academic Press.
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pubmed:issnType |
Print
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pubmed:volume |
12
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
867-73
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:10880230-Amino Acid Sequence,
pubmed-meshheading:10880230-Animals,
pubmed-meshheading:10880230-Binding Sites,
pubmed-meshheading:10880230-Biological Assay,
pubmed-meshheading:10880230-COS Cells,
pubmed-meshheading:10880230-Cell Line,
pubmed-meshheading:10880230-Fibronectins,
pubmed-meshheading:10880230-Humans,
pubmed-meshheading:10880230-Interleukin-5,
pubmed-meshheading:10880230-Mice,
pubmed-meshheading:10880230-Models, Molecular,
pubmed-meshheading:10880230-Molecular Sequence Data,
pubmed-meshheading:10880230-Protein Structure, Tertiary,
pubmed-meshheading:10880230-Receptors, Interleukin,
pubmed-meshheading:10880230-Receptors, Interleukin-5
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pubmed:year |
2000
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pubmed:articleTitle |
Identification of regions within the third FnIII-like domain of the IL-5Ralpha involved in IL-5 interaction.
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pubmed:affiliation |
Molecular Immunology Group, Curtin University of Technology, Perth, Australia. pczabot@nimr.mrc.ac.uk
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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