Linked Life Data

7600295

Source:http://linkedlifedata.com/resource/pubmed/id/7600295

Statements in which the resource exists.
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pubmed-article:7600295pubmed:abstractTextThe crystallographic structure of the MHC class II molecule showed that the alpha beta heterodimer can itself dimerize to form a four chain (alpha beta)2 complex of 120 kDa. Here we provide evidence for the existence of a 120 kDa (alpha beta)2 complex of the class II I-Ek molecules in mouse B cells. Both a 60 kDa and a 120 kDa form of I-Ek are detected by Western blotting and by immunoprecipitation under conditions in which class II alpha beta heterodimers are stable. The 120 kDa I-Ek complex does not contain Ii and, upon warming, dissociates into free alpha and beta chains. The 120 kDa I-Ek complex is expressed at the cell surface, is active in antigen presentation, and appears to play a significant role in T cell responses to low affinity but not to high affinity antigens, possibly by facilitating cross-linking of the T cell receptors.lld:pubmed
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pubmed-article:7600295pubmed:authorpubmed-author:PierceS KSKlld:pubmed
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pubmed-article:7600295pubmed:dateRevised2007-11-14lld:pubmed
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pubmed-article:7600295pubmed:articleTitleEvidence for dimers of MHC class II molecules in B lymphocytes and their role in low affinity T cell responses.lld:pubmed
pubmed-article:7600295pubmed:affiliationDepartment of Biochemistry, Molecular Biology, and Cell Biology, Northwestern University, Evanston, Illinois 60208, USA.lld:pubmed
pubmed-article:7600295pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:7600295pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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