170 Scopus citations


We have determined the crystal structure of I-A(g)7, an integral component in murine type I diabetes development. Several features distinguish I-A(g)7 from other non-autoimmune-associated MHC class II molecules, including novel peptide and heterodimer pairing interactions. The binding groove of I-A(g)7 is unusual at both terminal ends, with a potentially solvent-exposed channel at the base of the P1 pocket and a widened entrance to the P9 pocket. Peptide binding studies with variants of the hen egg lysozyme I-A(g)7 epitope HEL(11-25) support a comprehensive structure-based I-A(g)7 binding motif. Residues critical for T cell recognition were investigated with a panel of HEL(11-25)-restricted clones, which uncovered P1 anchor-dependent structural variations. These results establish a framework for future experiments directed at understanding the role of I-A(g)7 in autoimmunity.

Original languageEnglish
Pages (from-to)699-710
Number of pages12
Issue number6
StatePublished - 2000


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