2VLJ

The Structural Dynamics and Energetics of an Immunodominant T-cell Receptor are Programmed by its Vbeta Domain

Summary for 2VLJ

• Entry DOI: 10.2210/pdb2vlj/pdb
• Related: 1A1M 1A1N 1A1O 1A6Z 1A9B 1A9E 1AGB 1AGC 1AGD 1AGE 1AGF 1AKJ 1AO7 1AQD 1B0G 1B0R 1BD2 1C16 1CE6 1CG9 1DE4 1DUY 1DUZ 1E27 1E28 1EEY 1EEZ 1EFX 1EXU 1GZP 1GZQ 1HHG 1HHH 1HHI 1HHJ 1HHK 1HLA 1HSA 1HSB 1I1F 1I1Y 1I4F 1I7R 1I7T 1I7U 1IM3 1IM9 1JF1 1JGD 1JGE 1JHT 1JNJ 1K5N 1KPR 1KTL 1LDS 1LP9 1M05 1M6O 1MHE 1MI5 1N2R 1OF2 1OGA 1OGT 1ONQ 1P7Q 1PY4 1Q94 1QEW 1QLF 1QQD 1QR1 1QRN 1QSE 1QSF 1QVO 1R3H 1S9W 1S9X 1S9Y 1SYS 1SYV 1TMC 1TVB 1TVH 1UQS 1UR7 1UXS 1UXW 1VGK 1W0V 1W0W 1W72 1X7Q 1XH3 1XR8 1XR9 1XZ0 1YDP 1YPZ 1ZS8 1ZSD 1ZT4 2A83 2AK4 2AV1 2AV7 2AXF 2AXG 2BCK 2BNQ 2BNR 2BSR 2BSS 2BST 2BSU 2BSV 2BVQ 2C7U 2CII 2CIK 2CLR 2D31 2F74 2F8O 2GJ6 2H26 2HJK 2HJL 2HLA 2J8U 2JCC 2UWE 2V2W 2V2X 2VB5 2VLK 2VLL 2VLM 3HLA
• Descriptor: HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, A-2 ALPHA CHAIN, BETA-2-MICROGLOBULIN, FLU MATRIX PEPTIDE, ... (6 entities in total)
• Functional Keywords: immune system, glycoprotein, transmembrane, immune system-receptor-complex, immunoglobulin domain, host-virus interaction, pyrrolidone carboxylic acid, immune response, immunodominance, disease mutation, membrane, secreted, receptor, glycation, tcr, flu, mhc, mhc i, t-cell, complex
• Biological source: HOMO SAPIENS (HUMAN); More
• Cellular location: Membrane; Single-pass type I membrane protein: P01892; Secreted: P61769
• Total number of polymer chains: 5
• Total formula weight: 94607.14

Authors

Ishizuka, J.,Stewart-Jones, G.,Van Der Merwe, A.,Bell, J.,Mcmichael, A.,Jones, Y. (deposition date: 2008-01-15, release date: 2008-01-22, Last modification date: 2011-07-13)

Primary citation

Ishizuka, J.,Stewart-Jones, G.,Van Der Merwe, A.,Bell, J.,Mcmichael, A.,Jones, Y.
The Structural Dynamics and Energetics of an Immunodominant T-Cell Receptor are Programmed by its Vbeta Domain
Immunity, 28:171-, 2008

PubMed Abstract: Immunodominant and public T cell receptor (TCR) usage is relatively common in many viral diseases yet surprising in the context of the large naive TCR repertoire. We examined the highly conserved Vbeta17:Valpha10.2 JM22 T cell response to the influenza matrix peptide (58-66)-HLA-A*0201 (HLA-A2-flu) through extensive kinetic, thermodynamic, and structural analyses. We found several conformational adjustments that accompany JM22-HLA-A2-flu binding and identified a binding "hotspot" within the Vbeta domain of the TCR. Within this hotspot, key germline-encoded CDR1 and CDR2 loop residues and a crucial but commonly coded residue in the hypervariable region of CDR3 provide the basis for the substantial bias in the selection of the germline-encoded Vbeta17 domain. The chances of having a substantial number of T cells in the naive repertoire that have HLA-A2-flu-specific Vbeta17 receptors may consequently be relatively high, thus explaining the immunodominant usage of this clonotype.

PubMed: 18275829
DOI: 10.1016/J.IMMUNI.2007.12.018

Experimental method

X-RAY DIFFRACTION (2.4 Å)