Summary for 2V2W
| Entry DOI | 10.2210/pdb2v2w/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 1S8D 1S9W 1S9X 1S9Y 1SYS 1SYV 1T1W 1T1X 1T1Y 1T1Z 1T20 1T21 1T22 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 2ESV 2F74 2F8O 2GJ6 2H26 2HJK 2HJL 2HLA 2JCC 2UWE 2V2X 3HLA |
| Descriptor | HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, A-2 ALPHA CHAIN, BETA-2 MICROGLOBULIN, HIV P17, ... (4 entities in total) |
| Functional Keywords | immunoglobulin domain, complex (antigen-peptide), tcr, hiv, mhc, aids, mhc i, hla-a2, membrane, host-virus interaction, pyrrolidone carboxylic acid, immune system, ubl conjugation, immune response, disease mutation, polymorphism, glycoprotein, transmembrane |
| Biological source | HOMO SAPIENS (HUMAN) More |
| Cellular location | Membrane; Single-pass type I membrane protein: P01892 Secreted: P61769 |
| Total number of polymer chains | 6 |
| Total formula weight | 89623.55 |
| Authors | Lee, J.K.,Stewart-Jones, G.,Dong, T.,Harlos, K.,Di Gleria, K.,Dorrell, L.,Douek, D.C.,Van Der Merwe, P.A.,Jones, E.Y.,Mcmichael, A.J. (deposition date: 2007-06-07, release date: 2007-11-06, Last modification date: 2023-12-13) |
| Primary citation | Lee, J.K.,Stewart-Jones, G.,Dong, T.,Harlos, K.,Di Gleria, K.,Dorrell, L.,Douek, D.C.,Van Der Merwe, P.A.,Jones, E.Y.,Mcmichael, A.J. T Cell Cross-Reactivity and Conformational Changes During Tcr Engagement. J.Exp.Med., 200:1455-, 2004 Cited by PubMed Abstract: All thymically selected T cells are inherently cross-reactive, yet many data indicate a fine specificity in antigen recognition, which enables virus escape from immune control by mutation in infections such as the human immunodeficiency virus (HIV). To address this paradox, we analyzed the fine specificity of T cells recognizing a human histocompatibility leukocyte antigen (HLA)-A2-restricted, strongly immunodominant, HIV gag epitope (SLFNTVATL). The majority of 171 variant peptides tested bound HLA-A2, but only one third were recognized. Surprisingly, one recognized variant (SLYNTVATL) showed marked differences in structure when bound to HLA-A2. T cell receptor (TCR) recognition of variants of these two peptides implied that they adopted the same conformation in the TCR-peptide-major histocompatibility complex (MHC) complex. However, the on-rate kinetics of TCR binding were identical, implying that conformational changes at the TCR-peptide-MHC binding interface occur after an initial permissive antigen contact. These findings have implications for the rational design of vaccines targeting viruses with unstable genomes. PubMed: 15583017DOI: 10.1084/JEM.20041251 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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