| pubmed-article:16181344 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16181344 | lifeskim:mentions | umls-concept:C0024518 | lld:lifeskim |
| pubmed-article:16181344 | lifeskim:mentions | umls-concept:C0683117 | lld:lifeskim |
| pubmed-article:16181344 | pubmed:dateCreated | 2005-9-26 | lld:pubmed |
| pubmed-article:16181344 | pubmed:abstractText | The relative plasticity of peptide binding to class II major histocompatibility complex (MHC) molecules permits formation of multiple conformational isomers by the same peptide and MHC molecule; such conformers are specifically recognized by distinct subsets of T cells. Here, we review current knowledge and recent advances in our understanding of peptide-class II MHC conformational isomerism and the mechanisms that generate distinct MHC-peptide conformers. We focus on our studies of two T-cell subsets, type A and B, which recognize distinct conformers of the dominant epitope of hen egg white lysozyme presented by I-A(k). These conformers form via different pathways and in distinct intracellular vesicles: the type A conformer forms in late endosomes upon processing of native protein, while the more flexible type B conformer forms in early endosomes and at the cell surface. In this process, H2-DM acts as a conformational editor, eliminating the type B conformer in late endosomes. Type B T cells constitute a significant component of the naïve T-cell repertoire; furthermore, self-reactive type B T cells escape negative selection and are present in abundance in the periphery. Ongoing studies should elucidate the role of type B T cells in immunity to pathogens and in autoimmune pathology. | lld:pubmed |
| pubmed-article:16181344 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16181344 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16181344 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16181344 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16181344 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16181344 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16181344 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16181344 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16181344 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:16181344 | pubmed:issn | 0105-2896 | lld:pubmed |
| pubmed-article:16181344 | pubmed:author | pubmed-author:UnanueEmil... | lld:pubmed |
| pubmed-article:16181344 | pubmed:author | pubmed-author:LovitchScott... | lld:pubmed |
| pubmed-article:16181344 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16181344 | pubmed:volume | 207 | lld:pubmed |
| pubmed-article:16181344 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16181344 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16181344 | pubmed:pagination | 293-313 | lld:pubmed |
| pubmed-article:16181344 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:16181344 | pubmed:meshHeading | pubmed-meshheading:16181344... | lld:pubmed |
| pubmed-article:16181344 | pubmed:meshHeading | pubmed-meshheading:16181344... | lld:pubmed |
| pubmed-article:16181344 | pubmed:meshHeading | pubmed-meshheading:16181344... | lld:pubmed |
| pubmed-article:16181344 | pubmed:meshHeading | pubmed-meshheading:16181344... | lld:pubmed |
| pubmed-article:16181344 | pubmed:meshHeading | pubmed-meshheading:16181344... | lld:pubmed |
| pubmed-article:16181344 | pubmed:meshHeading | pubmed-meshheading:16181344... | lld:pubmed |
| pubmed-article:16181344 | pubmed:meshHeading | pubmed-meshheading:16181344... | lld:pubmed |
| pubmed-article:16181344 | pubmed:meshHeading | pubmed-meshheading:16181344... | lld:pubmed |
| pubmed-article:16181344 | pubmed:meshHeading | pubmed-meshheading:16181344... | lld:pubmed |
| pubmed-article:16181344 | pubmed:meshHeading | pubmed-meshheading:16181344... | lld:pubmed |
| pubmed-article:16181344 | pubmed:meshHeading | pubmed-meshheading:16181344... | lld:pubmed |
| pubmed-article:16181344 | pubmed:meshHeading | pubmed-meshheading:16181344... | lld:pubmed |
| pubmed-article:16181344 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:16181344 | pubmed:articleTitle | Conformational isomers of a peptide-class II major histocompatibility complex. | lld:pubmed |
| pubmed-article:16181344 | pubmed:affiliation | Department of Pathology and Immunology, Washington University School of Medicine, St Louis, MO 63110, USA. | lld:pubmed |
| pubmed-article:16181344 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16181344 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:16181344 | pubmed:publicationType | Review | lld:pubmed |
| pubmed-article:16181344 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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