Source:http://linkedlifedata.com/resource/pubmed/id/10363718
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
1999-7-12
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pubmed:abstractText |
HLA class II molecules present antigenic peptides to the T cell receptor of CD4+ T lymphocytes and interact with CD4 during the antigen recognition process. A major CD4 binding site encompassing amino acids (aa) 134-148 in the beta 2 domain of HLA-DR has been previously identified and residues located within the alpha 2 subunit of murine MHC class II I-Ad molecules have been shown to contribute to CD4-class II interaction. To characterize the alpha 2 region of HLA-DR molecules involved in the binding of CD4, we have synthesized overlapping linear and cyclic peptides derived from a region encompassing aa 121-143. We demonstrate that two linear peptides (aa 124-138 and 130-143) and a cyclic one (aa 121-138) specifically bind to CD4-sepharose affinity columns. Although cyclic analogues exhibit more ordered populations as detected by circular dichroism measurements, cyclization did not improve the activity of some peptides. Peptide sequence positioning in HLA-DR1 dimer model indicates that alpha 2 residues 124 to 136 form a solvent-exposed loop which faces the beta 2 loop delimited by residues 134-148. These data suggest that one CD4 molecule contacts both alpha 2 and beta 2 loops of the HLA-DR homodimer.
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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 |
Apr
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pubmed:issn |
0198-8859
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
60
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
273-81
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:10363718-Amino Acid Sequence,
pubmed-meshheading:10363718-Antigens, CD4,
pubmed-meshheading:10363718-Chromatography, Affinity,
pubmed-meshheading:10363718-Circular Dichroism,
pubmed-meshheading:10363718-HLA-DR Antigens,
pubmed-meshheading:10363718-Humans,
pubmed-meshheading:10363718-Models, Molecular,
pubmed-meshheading:10363718-Molecular Sequence Data,
pubmed-meshheading:10363718-Peptide Fragments,
pubmed-meshheading:10363718-Protein Binding,
pubmed-meshheading:10363718-Sepharose
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pubmed:year |
1999
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pubmed:articleTitle |
Definition of the alpha 2 region of HLA-DR molecules involved in CD4 binding.
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pubmed:affiliation |
Génétique Moléculaire et de Biologie du Développement, UPR 420 Centre National de la Recherche Scientifique, Villejuif, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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