1F3J

HISTOCOMPATIBILITY ANTIGEN I-AG7

Summary for 1F3J

• Entry DOI: 10.2210/pdb1f3j/pdb
• Descriptor: H-2 CLASS II HISTOCOMPATIBILITY ANTIGEN, MHC CLASS II NOD, LYSOZYME C, ... (5 entities in total)
• Functional Keywords: histocompatibility antigen, mhc, peptide complex, immune system
• Biological source: Mus musculus (house mouse); More
• Total number of polymer chains: 6
• Total formula weight: 90615.08

Authors

Latek, R.R.,Unanue, E.R.,Fremont, D.H. (deposition date: 2000-06-04, release date: 2000-09-20, Last modification date: 2024-10-30)

Primary citation

Latek, R.R.,Suri, A.,Petzold, S.J.,Nelson, C.A.,Kanagawa, O.,Unanue, E.R.,Fremont, D.H.
Structural basis of peptide binding and presentation by the type I diabetes-associated MHC class II molecule of NOD mice.
Immunity, 12:699-710, 2000

PubMed Abstract: 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.

PubMed: 10894169
DOI: 10.1016/S1074-7613(00)80220-4

Experimental method

X-RAY DIFFRACTION (3.1 Å)