1K2D

Crystal structure of the autoimmune MHC class II I-Au complexed with myelin basic protein 1-11 at 2.2A

Summary for 1K2D

• Entry DOI: 10.2210/pdb1k2d/pdb
• Descriptor: H-2 class II histocompatibility antigen, A-U alpha chain, H-2 class II histocompatibility antigen, A-U beta chain, Myelin Basic Protein peptide with 8 residue linker peptide, ... (5 entities in total)
• Functional Keywords: mhc class ii, i-au, h-2u, autoimmune disease, unique register, experimental autoimmune encephalomyelitis, myelin basic protein, immune system
• Biological source: Mus musculus (house mouse); More
• Total number of polymer chains: 3
• Total formula weight: 46946.99

Authors

He, X.L.,Radu, C.,Ward, E.S.,Garcia, K.C. (deposition date: 2001-09-26, release date: 2003-03-04, Last modification date: 2024-10-16)

Primary citation

He, X.L.,Radu, C.,Sidney, J.,Sette, A.,Ward, E.S.,Garcia, K.C.
Structural snapshot of aberrant antigen presentation linked to autoimmunity: the immunodominant epitope of MBP complexed with I-Au
IMMUNITY, 17:83-94, 2002

PubMed Abstract: 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.

PubMed: 12150894
DOI: 10.1016/S1074-7613(02)00340-0

Experimental method

X-RAY DIFFRACTION (2.2 Å)