5IVX
Crystal Structure of B4.2.3 T-Cell Receptor and H2-Dd P18-I10 Complex
5IVX の概要
エントリーDOI | 10.2210/pdb5ivx/pdb |
関連するPDBエントリー | 5IW1 |
分子名称 | H-2 class I histocompatibility antigen, D-D alpha chain, Beta-2-microglobulin, T-CELL RECEPTOR ALPHA CHAIN, ... (7 entities in total) |
機能のキーワード | major histompatibility complex class i, mhc-i, h2-dd, h-2dd, t-cell receptor, tcr, b4.2.3, b423, immune response, viral immunoevasion, immune system, human immunodeficiency virus, molecular recognition |
由来する生物種 | Mus musculus (Mouse) 詳細 |
細胞内の位置 | Membrane; Single-pass type I membrane protein: P01900 Secreted: P01887 |
タンパク質・核酸の鎖数 | 5 |
化学式量合計 | 93877.44 |
構造登録者 | |
主引用文献 | Natarajan, K.,McShan, A.C.,Jiang, J.,Kumirov, V.K.,Wang, R.,Zhao, H.,Schuck, P.,Tilahun, M.E.,Boyd, L.F.,Ying, J.,Bax, A.,Margulies, D.H.,Sgourakis, N.G. An allosteric site in the T-cell receptor C beta domain plays a critical signalling role. Nat Commun, 8:15260-15260, 2017 Cited by PubMed Abstract: The molecular mechanism through which the interaction of a clonotypic αβ T-cell receptor (TCR) with a peptide-loaded major histocompatibility complex (p/MHC) leads to T-cell activation is not yet fully understood. Here we exploit a high-affinity TCR (B4.2.3) to examine the structural changes that accompany binding to its p/MHC ligand (P18-I10/H2-D). In addition to conformational changes in complementarity-determining regions (CDRs) of the TCR seen in comparison of unliganded and bound X-ray structures, NMR characterization of the TCR β-chain dynamics reveals significant chemical shift effects in sites removed from the MHC-binding site. Remodelling of electrostatic interactions near the Cβ H3 helix at the membrane-proximal face of the TCR, a region implicated in interactions with the CD3 co-receptor, suggests a possible role for an allosteric mechanism in TCR signalling. The contribution of these TCR residues to signal transduction is supported by mutagenesis and T-cell functional assays. PubMed: 28508865DOI: 10.1038/ncomms15260 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.1 Å) |
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