We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
A structural framework for deciphering the link between I-Ag7 and autoimmune diabetes.
- Authors
Corper, A L; Stratmann, T; Apostolopoulos, V; Scott, C A; Garcia, K C; Kang, A S; Wilson, I A; Teyton, L
- 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.
- Publication
Science (New York, N.Y.), 2000, Vol 288, Issue 5465, p505
- ISSN
0036-8075
- Publication type
Journal Article
- DOI
10.1126/science.288.5465.505