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• W2040252005 startingPage "699" @default.
• W2040252005 abstract "The crystallographic structure of the MHC class II molecule showed that the αβ heterodimer can itself dimerize to form a four chain (αβ)2 complex of 120 kDa. Here we provide evidence for the existence of a 120 kDa (αβ)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 αβ heterodimers are stable. The 120 kDa I-Ek complex does not contain li and, upon warming, dissociates into free α and β 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." @default.
• W2040252005 created "2016-06-24" @default.
• W2040252005 creator A5017572254 @default.
• W2040252005 creator A5025853358 @default.
• W2040252005 date "1994-11-01" @default.
• W2040252005 modified "2023-09-23" @default.
• W2040252005 title "Evidence for dimers of MHC class II molecules in B lymphocytes and their role in low affinity T cell responses" @default.
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• W2040252005 doi "https://doi.org/10.1016/1074-7613(94)90040-x" @default.
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