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Title: Alteration of a non-polymorphic residue in a class II E beta gene eliminates an antibody-defined epitope without affecting T cell recognition. Author: Griffith IJ, Carland FM, Glimcher LH. Journal: J Immunol; 1987 Jun 15; 138(12):4480-3. PubMed ID: 2438346. Abstract: The interaction between the clonally selected T cell receptor, antigen, and Ia molecule is poorly understood at the molecular level. A cell line bearing an altered E beta k molecule has been examined to provide more information about the relationship between Ia structure and function. The cell line, 2B1, was derived from the TA3 B cell hybridoma through a series of negative and positive immunoselection steps. The 2B1 mutant lacked the binding site recognized by the 17.3.3 monoclonal antibody (mAb) but presented antigen normally to all I-Ek-restricted T cell hybridomas and clones examined. Sequence analysis of the mutant E beta k gene showed a single base transition (G----A) that resulted in an arginine to a histidine substitution at amino acid 49 of the beta 1 domain. This mutation demonstrates that residue 49 is not involved in antigen presentation to T cells but can be involved in B cell recognition (mAb binding).[Abstract] [Full Text] [Related] [New Search]