Differential binding of peptides substituted at a putative C-terminal anchor residue to I-A super(g7) beta super(56)His beta super(57)Ser and I-A super(g7) beta super(56)Pro beta super(57)Asp
Susceptibility to insulin-dependent diabetes mellitus (IDDM), an autoimmune disease resulting in the selective destruction of islet beta cells in the pancreas, is associated with certain HLA alleles. Todd and co-workers (1987) hypothesized that susceptibility to IDDM was associated with the amino ac...
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Published in | Immunogenetics (New York) Vol. 47; no. 5; pp. 411 - 414 |
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Main Authors | , , , , , , , |
Format | Journal Article |
Language | English |
Published |
01.04.1998
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Online Access | Get full text |
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Summary: | Susceptibility to insulin-dependent diabetes mellitus (IDDM), an autoimmune disease resulting in the selective destruction of islet beta cells in the pancreas, is associated with certain HLA alleles. Todd and co-workers (1987) hypothesized that susceptibility to IDDM was associated with the amino acid residue at position 57 of DQ beta (DQ beta super(57)), with non-Asp being susceptible and Asp being non-susceptible to IDDM. In our previous studies, we determined the binding peptide motifs for DQ8 (DQ beta super(57)Ala; IDDM-susceptible) and DQ9 (I-A beta super(57)Asp; IDDM-non-susceptible), and found significant differences between DQ9 and DQ8, in that the majority of polar residues, regardless of their static charges at the putative C-terminal anchor residue, permitted binding to IDDM-susceptible DQ8, which is not the case for DQ9. In the current study, we used mouse IDDM-susceptible I-A (I-A super(g7) beta super(56)His beta super(57)Ser) and IDDM-non-susceptible mutated I-A (I-A super(g7) beta super(56)Pro beta super(57)Asp) molecules, to determine whether the same rule applies for peptide binding. |
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Bibliography: | ObjectType-Article-2 SourceType-Scholarly Journals-1 content type line 23 ObjectType-Feature-1 |
ISSN: | 0093-7711 |