2BSR

Crystal structures and KIR3DL1 recognition of three immunodominant viral peptides complexed to HLA-B2705

Summary for 2BSR

• Entry DOI: 10.2210/pdb2bsr/pdb
• Related: 1A1M 1A1N 1A1O 1A6Z 1A9B 1A9E 1AGB 1AGC 1AGD 1AGE 1AGF 1AKJ 1AO7 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 1ROG 1ROH 1ROI 1ROJ 1ROK 1ROL 1S9W 1S9X 1S9Y 1SYS 1SYV 1TMC 1TVB 1TVH 1UQS 1UR7 1UXS 1UXW 1W0V 1W0W 1W72 1XH3 1XR8 1XR9 1XZ0 1YDP 1YPZ 2BNQ 2BNR 2BSS 2BST 2CLR 2HLA 3HLA
• Descriptor: HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, B-27 ALPHA CHAIN PRECURSOR, BETA-2-MICROGLOBULIN, EPSTEIN-BARR NUCLEAR ANTIGEN-6, ... (4 entities in total)
• Functional Keywords: immune system/peptide, mhc, hla-b27, human ebv, hiv, glycoprotein, mhc i, polymorphism, transmembrane, immunoglobulin domain, pyrrolidone carboxylic acid, nuclear protein, complex (antigen-peptide), immune system-peptide complex
• Biological source: HOMO SAPIENS (HUMAN); More
• Cellular location: Membrane; Single-pass type I membrane protein: P03989; Secreted: P61769; Host nucleus matrix: P03204
• Total number of polymer chains: 3
• Total formula weight: 44998.94

Authors

Stewart-Jones, G.B.E.,Di Gleria, K.,Kollnberger, S.,Mcmichael, A.J.,Jones, E.Y.,Bowness, P. (deposition date: 2005-05-23, release date: 2005-05-24, Last modification date: 2011-07-13)

Primary citation

Stewart-Jones, G.B.E.,Di Gleria, K.,Kollnberger, S.,Mcmichael, A.J.,Jones, E.Y.,Bowness, P.
Crystal Structures and Kir3Dl1 Recognition of Three Immunodominant Viral Peptides Complexed to Hla-B2705
Eur.J.Immunol., 35:341-, 2005

PubMed Abstract: We have solved the crystal structures of three HLA-B*2705-peptide complexes with the immunodominant viral peptides: EBV EBNA3C 258-266 (RRIYDLIEL), influenza (flu) nucleoprotein NP383-391 (SRYWAIRTR), and HIV gag 264-273 (KRWIILGLNK). Long-term non-progression during HIV infection has been associated with presentation by HLA-B*2705, and T cell recognition, of the highly immunodominant KRWIILGLNK peptide. The tight hydrogen-bonding network observed between the HLA-B*2705 B-pocket and the peptide P2 arginine guanadinium anchor explains why mutation of this residue during HIV infection results in loss of peptide binding, immune escape and progression to AIDS. Prominent, solvent-exposed structures within these peptides may participate in generating T cell responses to these immunodominant epitopes. In the HLA-B*2705 complex with flu NP383-391, the amino acid side chains of residues 4, 7 and 8 are solvent-exposed whilst in the HIV decamer, the main-chain bulges into the solvent around P7. Thus, HLA-B*2705 presents viral peptides in a range of conformations. Tetrameric complexes of HLA-B*2705 with the HIV and flu but not EBV peptides bound strongly to the killer-Ig-like receptor (KIR)3DL1. Substitution of EBV P8 glutamate to threonine allowed recognition by KIR3DL1. In the HLA-B*2705-EBV structure the P8 glutamate side chain is solvent-exposed and may inhibit KIR3DL1 binding through electrostatic forces.

PubMed: 15657948
DOI: 10.1002/EJI.200425724

Experimental method

X-RAY DIFFRACTION (2.3 Å)