1ES0

CRYSTAL STRUCTURE OF THE MURINE CLASS II ALLELE I-A(G7) COMPLEXED WITH THE GLUTAMIC ACID DECARBOXYLASE (GAD65) PEPTIDE 207-220

Summary for 1ES0

• Entry DOI: 10.2210/pdb1es0/pdb
• Descriptor: H-2 CLASS II HISTOCOMPATIBILITY ANTIGEN, 65 KD GLUTAMIC ACID DECARBOXYLASE+H-2 CLASS II HISTOCOMPATIBILITY ANTIGEN (3 entities in total)
• Functional Keywords: histocompatibility antigen, class ii mhc i-a(g7), immune system
• Biological source: Mus musculus (mouse); More
• Cellular location: Membrane ; Single-pass type I membrane protein : P04228
• Total number of polymer chains: 2
• Total formula weight: 47186.56

Authors

Corper, A.L.,Teyton, L.,Wilson, I.A. (deposition date: 2000-04-07, release date: 2000-06-28, Last modification date: 2024-10-09)

Primary citation

Corper, A.L.,Stratmann, T.,Apostolopoulos, V.,Scott, C.A.,Garcia, K.C.,Kang, A.S.,Wilson, I.A.,Teyton, L.
A structural framework for deciphering the link between I-Ag7 and autoimmune diabetes.
Science, 288:505-511, 2000

PubMed Abstract: Susceptibility to murine and human insulin-dependent diabetes mellitus correlates strongly with major histocompatibility complex (MHC) class II I-A or HLA-DQ alleles that lack an aspartic acid at position beta57. I-Ag7 lacks this aspartate and is the only class II allele expressed by the nonobese diabetic mouse. The crystal structure of I-Ag7 was determined at 2.6 angstrom resolution as a complex with a high-affinity peptide from the autoantigen glutamic acid decarboxylase (GAD) 65. I-Ag7 has a substantially wider peptide-binding groove around beta57, which accounts for distinct peptide preferences compared with other MHC class II alleles. Loss of Asp(beta57) leads to an oxyanion hole in I-Ag7 that can be filled by peptide carboxyl residues or, perhaps, through interaction with the T cell receptor.

PubMed: 10775108
DOI: 10.1126/science.288.5465.505

Experimental method

X-RAY DIFFRACTION (2.6 Å)