3PGC
Crystal Structure of HLA-DR1 with CLIP106-120, flipped peptide orientation
3PGC の概要
エントリーDOI | 10.2210/pdb3pgc/pdb |
関連するPDBエントリー | 3PDO 3PGD |
分子名称 | HLA class II histocompatibility antigen, DR alpha chain, HLA class II histocompatibility antigen, DRB1-1 beta chain, HLA class II histocompatibility antigen gamma chain, ... (6 entities in total) |
機能のキーワード | mhc class ii, mhc ii, immune system, self antigen, invariant chain, clip |
由来する生物種 | Homo sapiens (human) 詳細 |
細胞内の位置 | Cell membrane; Single-pass type I membrane protein: P01903 P04229 Cell membrane; Single-pass type II membrane protein (Potential): P04233 |
タンパク質・核酸の鎖数 | 6 |
化学式量合計 | 94548.77 |
構造登録者 | Gunther, S.,Schlundt, A.,Sticht, J.,Roske, Y.,Heinemann, U.,Wiesmuller, K.-H.,Jung, G.,Falk, K.,Rotzschke, O.,Freund, C. (登録日: 2010-11-01, 公開日: 2010-12-08, 最終更新日: 2024-11-27) |
主引用文献 | Gunther, S.,Schlundt, A.,Sticht, J.,Roske, Y.,Heinemann, U.,Wiesmuller, K.H.,Jung, G.,Falk, K.,Rotzschke, O.,Freund, C. Bidirectional binding of invariant chain peptides to an MHC class II molecule. Proc.Natl.Acad.Sci.USA, 107:22219-22224, 2010 Cited by PubMed Abstract: T-cell recognition of peptides bound to MHC class II (MHCII) molecules is a central event in cell-mediated adaptive immunity. The current paradigm holds that prebound class II-associated invariant chain peptides (CLIP) and all subsequent antigens maintain a canonical orientation in the MHCII binding groove. Here we provide evidence for MHCII-bound CLIP inversion. NMR spectroscopy demonstrates that the interconversion from the canonical to the inverse alignment is a dynamic process, and X-ray crystallography shows that conserved MHC residues form a hydrogen bond network with the peptide backbone in both orientations. The natural catalyst HLA-DM accelerates peptide reorientation and the exchange of either canonically or inversely bound CLIP against antigenic peptide. Thus, noncanonical MHC-CLIP displays the hallmarks of a structurally and functionally intact antigen-presenting complex. PubMed: 21115828DOI: 10.1073/pnas.1014708107 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.66 Å) |
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