1OGA

A structural basis for immunodominant human T-cell receptor recognition.

Summary for 1OGA

• Entry DOI: 10.2210/pdb1oga/pdb
• Related: 1A1M 1A1N 1A1O 1A6Z 1A9B 1A9E 1AGB 1AGC 1AGD 1AGE 1AGF 1AKJ 1AO7 1B0G 1B0R 1BD2 1CE6 1DE4 1DUY 1DUZ 1E27 1E28 1EFX 1EXU 1FYT 1GZP 1GZQ 1HHG 1HHH 1HHI 1HHJ 1HHK 1HLA 1HSA 1HSB 1I1F 1I1Y 1I4F 1I7R 1I7T 1I7U 1IM3 1IM9 1JF1 1JGE 1JHT 1JNJ 1K5N 1KGC 1KPR 1KTL 1LDS 1OF2 1QLF 1QQD 1QR1 1QRN 1QSE 1QSF 1TMC 2CLR 2HLA 3HLA
• Descriptor: HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, BETA-2-MICROGLOBULIN, GILGFVFTL, ... (6 entities in total)
• Functional Keywords: immune system/receptor, immune system-receptor-complex, tcr, mhc, immunodominance, flu, complex, transmembrane, glycoprotein, polymorphism, t-cell, receptor, immune system-receptor complex
• Biological source: HOMO SAPIENS (HUMAN); More
• Cellular location: Membrane; Single-pass type I membrane protein: P01892; Secreted: P01884
• Total number of polymer chains: 5
• Total formula weight: 96955.54

Authors

Stewart-Jones, G.B.E.,McMichael, A.J.,Bell, J.I.,Stuart, D.I.,Jones, E.Y. (deposition date: 2003-04-28, release date: 2003-06-19, Last modification date: 2024-11-06)

Primary citation

Stewart-Jones, G.B.E.,Mcmichael, A.J.,Bell, J.I.,Stuart, D.I.,Jones, E.Y.
A Structural Basis for Immunodominant Human T Cell Receptor Recognition
Nat.Immunol., 4:657-, 2003

PubMed Abstract: The anti-influenza CD8+ T cell response in HLA-A2-positive adults is almost exclusively directed at residues 58-66 of the virus matrix protein (MP(58-66)). V(beta)17V(alpha)10.2 T cell receptors (TCRs) containing a conserved arginine-serine-serine sequence in complementarity determining region 3 (CDR3) of the V(beta) segment dominate this response. To investigate the molecular basis of immunodominant selection in an outbred population, we have determined the crystal structure of V(beta)17V(alpha)10.2 in complex with MP(58-66)-HLA-A2 at a resolution of 1.4 A. We show that, whereas the TCR typically fits over an exposed side chain of the peptide, in this structure MP(58-66) exposes only main chain atoms. This distinctive orientation of V(beta)17V(alpha)10.2, which is almost orthogonal to the peptide-binding groove of HLA-A2, facilitates insertion of the conserved arginine in V(beta) CDR3 into a notch in the surface of MP(58-66)-HLA-A2. This previously unknown binding mode underlies the immunodominant T cell response.

PubMed: 12796775
DOI: 10.1038/NI942

Experimental method

X-RAY DIFFRACTION (1.4 Å)