| First Author | Latek RR | Year | 2000 |
| Journal | Immunity | Volume | 12 |
| Issue | 6 | Pages | 699-710 |
| PubMed ID | 10894169 | Mgi Jnum | J:63051 |
| Mgi Id | MGI:1860371 | Doi | 10.1016/s1074-7613(00)80220-4 |
| Citation | Latek RR, et al. (2000) Structural basis of peptide binding and presentation by the type I diabetes-associated MHC class II molecule of NOD mice. Immunity 12(6):699-710 |
| abstractText | 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. |
