1K2D

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

1K2D の概要

• エントリーDOI: 10.2210/pdb1k2d/pdb
• 分子名称: 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)
• 機能のキーワード: mhc class ii, i-au, h-2u, autoimmune disease, unique register, experimental autoimmune encephalomyelitis, myelin basic protein, immune system
• 由来する生物種: Mus musculus (house mouse); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 46946.99

構造登録者

He, X.L.,Radu, C.,Ward, E.S.,Garcia, K.C. (登録日: 2001-09-26, 公開日: 2003-03-04, 最終更新日: 2024-10-16)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.2 Å)