1k2d
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(New page: 200px<br /><applet load="1k2d" size="450" color="white" frame="true" align="right" spinBox="true" caption="1k2d, resolution 2.2Å" /> '''Crystal structure of ...)
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Revision as of 16:40, 20 November 2007
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Crystal structure of the autoimmune MHC class II I-Au complexed with myelin basic protein 1-11 at 2.2A
Overview
Murine experimental allergic encephalomyelitis (EAE) is a useful model for, the demyelinating, autoimmune disease multiple sclerosis. In the EAE, system, the immunodominant N-terminal epitope of myelin basic protein, (MBP) is an unusually short, weakly binding peptide antigen which elicits, highly biased TCR chain usage. In the 2.2 A crystal structure of, I-A(u)/MBP1-11 complex, only MBP residues 1-7 are bound toward one end of, the peptide binding cleft. The fourth residue of MBP1-11 is located in an, incompatible p6 pocket of I-A(u), thus explaining the short half-life of, I-A(u) complexed with Ac1-11. MBP peptides extended at the C terminus of, Ac1-11 result in dramatic affinity increases, likely attributed to, register shifting to a higher affinity cryptic epitope, which could, potentially mask the presentation of the immunodominant MBP1-11 peptide, during thymic education.
About this Structure
1K2D is a Protein complex structure of sequences from Mus musculus with NDG and NAG as ligands. Full crystallographic information is available from OCA.
Reference
Structural snapshot of aberrant antigen presentation linked to autoimmunity: the immunodominant epitope of MBP complexed with I-Au., He XL, Radu C, Sidney J, Sette A, Ward ES, Garcia KC, Immunity. 2002 Jul;17(1):83-94. PMID:12150894
Page seeded by OCA on Tue Nov 20 18:47:31 2007
