1f3j
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HISTOCOMPATIBILITY ANTIGEN I-AG7
OverviewOverview
We have determined the crystal structure of I-Ag7, an integral component, in murine type I diabetes development. Several features distinguish I-Ag7, from other non-autoimmune-associated MHC class II molecules, including, novel peptide and heterodimer pairing interactions. The binding groove of, I-Ag7 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-Ag7 epitope HEL(11-25) support a comprehensive structure-based I-Ag7, 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-Ag7 in autoimmunity.
About this StructureAbout this Structure
1F3J is a Protein complex structure of sequences from Gallus gallus and Mus musculus with NAG as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Structural basis of peptide binding and presentation by the type I diabetes-associated MHC class II molecule of NOD mice., Latek RR, Suri A, Petzold SJ, Nelson CA, Kanagawa O, Unanue ER, Fremont DH, Immunity. 2000 Jun;12(6):699-710. PMID:10894169
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