1es0
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(New page: 200px<br /><applet load="1es0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1es0, resolution 2.60Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 12:08, 20 November 2007
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CRYSTAL STRUCTURE OF THE MURINE CLASS II ALLELE I-A(G7) COMPLEXED WITH THE GLUTAMIC ACID DECARBOXYLASE (GAD65) PEPTIDE 207-220
Overview
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.
About this Structure
1ES0 is a Protein complex structure of sequences from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA.
Reference
A structural framework for deciphering the link between I-Ag7 and autoimmune diabetes., Corper AL, Stratmann T, Apostolopoulos V, Scott CA, Garcia KC, Kang AS, Wilson IA, Teyton L, Science. 2000 Apr 21;288(5465):505-11. PMID:10775108
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