3CVI
How TCR-like antibody recognizes MHC-bound peptide
3CVI の概要
| エントリーDOI | 10.2210/pdb3cvi/pdb |
| 関連するPDBエントリー | 3CVH |
| 分子名称 | 25-D1.16 Heavy chain, 25-D1.16 Light chain (3 entities in total) |
| 機能のキーワード | fab, immune system |
| 由来する生物種 | Mus musculus (mouse) 詳細 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 46636.00 |
| 構造登録者 | |
| 主引用文献 | Mareeva, T.,Martinez-Hackert, E.,Sykulev, Y. How a T cell receptor-like antibody recognizes major histocompatibility complex-bound peptide J.Biol.Chem., 283:29053-29059, 2008 Cited by PubMed Abstract: We determined the crystal structures of the T cell receptor (TCR)-like antibody 25-D1.16 Fab fragment bound to a complex of SIINFEKL peptide from ovalbumin and the H-2K(b) molecule. Remarkably, this antibody directly "reads" the structure of the major histocompatibility complex (MHC)-bound peptide, employing the canonical diagonal binding mode utilized by most TCRs. This is in marked contrast with another TCR-like antibody, Hyb3, bound to melanoma peptide MAGE-A1 in association with HLA-A1 MHC class I. Hyb3 assumes a non-canonical orientation over its cognate peptide-MHC and appears to recognize a conformational epitope in which the MHC contribution is dominant. We conclude that TCR-like antibodies can recognize MHC-bound peptide via two different mechanisms: one is similar to that exploited by the preponderance of TCRs and the other requires a non-canonical antibody orientation over the peptide-MHC complex. PubMed: 18703505DOI: 10.1074/jbc.M804996200 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.8 Å) |
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