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1D9K

CRYSTAL STRUCTURE OF COMPLEX BETWEEN D10 TCR AND PMHC I-AK/CA

1D9K の概要
エントリーDOI10.2210/pdb1d9k/pdb
分子名称T-CELL RECEPTOR D10 (ALPHA CHAIN), T-CELL RECEPTOR D10 (BETA CHAIN), MHC I-AK A CHAIN (ALPHA CHAIN), ... (7 entities in total)
機能のキーワードt-cell receptor, mhc class ii, d10, i-ak, 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10
化学式量合計141227.13
構造登録者
主引用文献Reinherz, E.L.,Tan, K.,Tang, L.,Kern, P.,Liu, J.,Xiong, Y.,Hussey, R.E.,Smolyar, A.,Hare, B.,Zhang, R.,Joachimiak, A.,Chang, H.C.,Wagner, G.,Wang, J.
The crystal structure of a T cell receptor in complex with peptide and MHC class II.
Science, 286:1913-1921, 1999
Cited by
PubMed Abstract: The crystal structure of a complex involving the D10 T cell receptor (TCR), 16-residue foreign peptide antigen, and the I-Ak self major histocompatibility complex (MHC) class II molecule is reported at 3.2 angstrom resolution. The D10 TCR is oriented in an orthogonal mode relative to its peptide-MHC (pMHC) ligand, necessitated by the amino-terminal extension of peptide residues projecting from the MHC class II antigen-binding groove as part of a mini beta sheet. Consequently, the disposition of D10 complementarity-determining region loops is altered relative to that of most pMHCI-specific TCRs; the latter TCRs assume a diagonal orientation, although with substantial variability. Peptide recognition, which involves P-1 to P8 residues, is dominated by the Valpha domain, which also binds to the class II MHC beta1 helix. That docking is limited to one segment of MHC-bound peptide offers an explanation for epitope recognition and altered peptide ligand effects, suggests a structural basis for alloreactivity, and illustrates how bacterial superantigens can span the TCR-pMHCII surface.
PubMed: 10583947
DOI: 10.1126/science.286.5446.1913
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (3.2 Å)
構造検証レポート
Validation report summary of 1d9k
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-12-31に公開中

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