1FO0

MURINE ALLOREACTIVE SCFV TCR-PEPTIDE-MHC CLASS I MOLECULE COMPLEX

1FO0 の概要

• エントリーDOI: 10.2210/pdb1fo0/pdb
• 分子名称: PROTEIN (ALLOGENEIC H-2KB MHC CLASS I MOLECULE), PROTEIN (BETA-2 MICROGLOBULIN), NATURALLY PROCESSED OCTAPEPTIDE PBM1, ... (6 entities in total)
• 機能のキーワード: t cell receptor, class i mhc, h-2kb, tcr-pmhc complex, immune system
• 由来する生物種: Mus musculus (house mouse); 詳細
• 細胞内の位置: Membrane; Single-pass type I membrane protein: P01901; Secreted: P01887
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 70507.53

構造登録者

Reiser, J.B.,Darnault, C.,Guimezanes, A.,Gregoire, C.,Mosser, T.,Schmitt-Verhulst, A.-M.,Fontecilla-Camps, J.C.,Malissen, B.,Housset, D.,Mazza, G. (登録日: 2000-08-24, 公開日: 2000-10-02, 最終更新日: 2024-11-13)

主引用文献

Reiser, J.B.,Darnault, C.,Guimezanes, A.,Gregoire, C.,Mosser, T.,Schmitt-Verhulst, A.-M.,Fontecilla-Camps, J.C.,Malissen, B.,Housset, D.,Mazza, G.
Crystal structure of a T cell receptor bound to an allogeneic MHC molecule.
Nat.Immunol., 1:291-297, 2000

PubMed Abstract: Many T cell receptors (TCRs) that are selected to respond to foreign peptide antigens bound to self major histocompatibility complex (MHC) molecules are also reactive with allelic variants of self-MHC molecules. This property, termed alloreactivity, causes graft rejection and graft-versus-host disease. The structural features of alloreactivity have yet to be defined. We now present a basis for this cross-reactivity, elucidated by the crystal structure of a complex involving the BM3.3 TCR and a naturally processed octapeptide bound to the H-2Kb allogeneic MHC class I molecule. A distinguishing feature of this complex is that the eleven-residue-long complementarity-determining region 3 (CDR3) found in the BM3.3 TCR alpha chain folds away from the peptide binding groove and makes no contact with the bound peptide, the latter being exclusively contacted by the BM3.3 CDR3 beta. Our results formally establish that peptide-specific, alloreactive TCRs interact with allo-MHC in a register similar to the one they use to contact self-MHC molecules.

PubMed: 11017099
DOI: 10.1038/79728

実験手法

X-RAY DIFFRACTION (2.5 Å)