2X4U

Crystal structure of MHC CLass I HLA-A2.1 bound to HIV-1 Peptide RT468-476

Summary for 2X4U

• Entry DOI: 10.2210/pdb2x4u/pdb
• Related: 1A1M 1A1N 1A1O 1A6Z 1A9B 1A9E 1A9M 1AGB 1AGC 1AGD 1AGE 1AGF 1AJV 1AJX 1AKJ 1AO7 1AQD 1AXA 1B0G 1B0R 1BD2 1BQM 1BQN 1C16 1CE6 1CG9 1D4H 1D4I 1D4J 1DE4 1DLO 1DUY 1DUZ 1DW6 1E27 1E28 1EBK 1EBW 1EBY 1EBZ 1EC0 1EC1 1EC2 1EC3 1EET 1EEY 1EEZ 1EFX 1EXU 1GZP 1GZQ 1HAR 1HBV 1HEF 1HEG 1HHG 1HHH 1HHI 1HHJ 1HHK 1HIH 1HLA 1HMV 1HNI 1HNV 1HOS 1HPS 1HPZ 1HQE 1HQU 1HRH 1HSA 1HSB 1HTE 1HTF 1HTG 1HVK 1HVP 1HVU 1HYS 1I1F 1I1Y 1I4F 1I7R 1I7T 1I7U 1IKV 1IKW 1IKX 1IKY 1IM3 1IM9 1J5O 1JF1 1JGD 1JGE 1JHT 1JNJ 1K5N 1KPR 1KTL 1LDS 1LP9 1M05 1M6O 1MER 1MES 1MET 1MEU 1MHE 1MI5 1N5Y 1N6Q 1NPA 1NPV 1NPW 1OF2 1OGA 1OGT 1ONQ 1P7Q 1PY4 1Q94 1QE1 1QEW 1QLF 1QMC 1QQD 1QR1 1QRN 1QSE 1QSF 1QVO 1R0A 1R3H 1RDH 1RTD 1RVL 1RVM 1RVN 1RVO 1RVP 1RVQ 1RVR 1S6P 1S6Q 1S9E 1S9G 1S9W 1S9X 1S9Y 1SBG 1SUQ 1SV5 1SYS 1SYV 1T03 1T05 1T7K 1TMC 1TV6 1TVB 1TVH 1TVR 1UQS 1UR7 1UWB 1UXS 1UXW 1VGK 1W0V 1W0W 1W5V 1W5W 1W5X 1W5Y 1W72 1X7Q 1XH3 1XR8 1XR9 1XZ0 1YDP 1YPZ 1YT9 1ZS8 1ZSD 1ZT4 2A83 2AK4 2AV1 2AV7 2AXF 2AXG 2B5J 2B6A 2BAN 2BBB 2BCK 2BE2 2BNQ 2BNR 2BSR 2BSS 2BST 2BVO 2BVP 2BVQ 2C7U 2CII 2CIK 2CLR 2D31 2ESV 2F74 2F8O 2GJ6 2H26 2HJK 2HJL 2HLA 2HMI 2J8U 2JCC 2UWE 2UXZ 2UY0 2V2W 2V2X 2VB5 2VG5 2VG6 2VG7 2VLJ 2VLK 2VLL 2VLR 2X4M 2X4N 2X4O 2X4P 2X4Q 2X4R 2X4S 2X4T 3HLA 3HVT 3TLH
• Descriptor: HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, A-2 ALPHA CHAIN, BETA-2-MICROGLOBULIN, REVERSE TRANSCRIPTASE/RIBONUCLEASE H, ... (6 entities in total)
• Functional Keywords: glycoprotein, immune system, transmembrane, phosphoprotein, immune response, secreted, glycation, amyloidosis, immunoglobulin domain, host-virus interaction, amyloid, membrane, photocleavable peptide, pyrrolidone carboxylic acid, envelope protein, disease mutation
• Biological source: HOMO SAPIENS (HUMAN); More
• Total number of polymer chains: 6
• Total formula weight: 91258.55

Authors

Celie, P.H.N.,Toebes, M.,Rodenko, B.,Ovaa, H.,Perrakis, A.,Schumacher, T.N.M. (deposition date: 2010-02-02, release date: 2010-03-02, Last modification date: 2024-11-06)

Primary citation

Celie, P.H.N.,Toebes, M.,Rodenko, B.,Ovaa, H.,Perrakis, A.,Schumacher, T.N.M.
Uv-Induced Ligand Exchange in Mhc Class I Protein Crystals.
J.Am.Chem.Soc., 131:12298-, 2009

PubMed Abstract: High-throughput structure determination of protein-ligand complexes is central in drug development and structural proteomics. To facilitate such high-throughput structure determination we designed an induced replacement strategy. Crystals of a protein complex bound to a photosensitive ligand are exposed to UV light, inducing the departure of the bound ligand, allowing a new ligand to soak in. We exemplify the approach for a class of protein complexes that is especially recalcitrant to high-throughput strategies: the MHC class I proteins. We developed a UV-sensitive, "conditional", peptide ligand whose UV-induced cleavage in the crystals leads to the exchange of the low-affinity lytic fragments for full-length peptides introduced in the crystallant solution. This "in crystallo" exchange is monitored by the loss of seleno-methionine anomalous diffraction signal of the conditional peptide compared to the signal of labeled MHC beta2m subunit. This method has the potential to facilitate high-throughput crystallography in various protein families.

PubMed: 19655750
DOI: 10.1021/JA9037559

Experimental method

X-RAY DIFFRACTION (2.1 Å)