2v2x
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1akj|1AKJ]], [[1ao7|1AO7]], [[1aqd|1AQD]], [[1b0g|1B0G]], [[1b0r|1B0R]], [[1bd2|1BD2]], [[1duy|1DUY]], [[1duz|1DUZ]], [[1eey|1EEY]], [[1eez|1EEZ]], [[1hhg|1HHG]], [[1hhh|1HHH]], [[1hhi|1HHI]], [[1hhj|1HHJ]], [[1hhk|1HHK]], [[1hla|1HLA]], [[1i1f|1I1F]], [[1i1y|1I1Y]], [[1i4f|1I4F]], [[1i7r|1I7R]], [[1i7t|1I7T]], [[1i7u|1I7U]], [[1im3|1IM3]], [[1jf1|1JF1]], [[1jht|1JHT]], [[1lp9|1LP9]], [[1oga|1OGA]], [[1p7q|1P7Q]], [[1qew|1QEW]], [[1qr1|1QR1]], [[1qrn|1QRN]], [[1qse|1QSE]], [[1qsf|1QSF]], [[1s8d|1S8D]], [[1s9w|1S9W]], [[1s9x|1S9X]], [[1s9y|1S9Y]], [[1t1w|1T1W]], [[1t1x|1T1X]], [[1t1y|1T1Y]], [[1t1z|1T1Z]], [[1t20|1T20]], [[1t21|1T21]], [[1t22|1T22]], [[1tvb|1TVB]], [[1tvh|1TVH]], [[1ur7|1UR7]], [[2av1|2AV1]], [[2av7|2AV7]], [[2bnq|2BNQ]], [[2bnr|2BNR]], [[2bsu|2BSU]], [[2bsv|2BSV]], [[2c7u|2C7U]], [[2clr|2CLR]], [[2gj6|2GJ6]], [[2jcc|2JCC]], [[2uwe|2UWE]], [[3hla|3HLA]], [[1a1m|1A1M]], [[1a1n|1A1N]], [[1a1o|1A1O]], [[1a6z|1A6Z]], [[1a9b|1A9B]], [[1a9e|1A9E]], [[1agb|1AGB]], [[1agc|1AGC]], [[1agd|1AGD]], [[1age|1AGE]], [[1agf|1AGF]], [[1c16|1C16]], [[1ce6|1CE6]], [[1cg9|1CG9]], [[1de4|1DE4]], [[1e27|1E27]], [[1e28|1E28]], [[1efx|1EFX]], [[1exu|1EXU]], [[1gzp|1GZP]], [[1gzq|1GZQ]], [[1hsa|1HSA]], [[1hsb|1HSB]], [[1im9|1IM9]], [[1jgd|1JGD]], [[1jge|1JGE]], [[1jnj|1JNJ]], [[1k5n|1K5N]], [[1kpr|1KPR]], [[1ktl|1KTL]], [[1lds|1LDS]], [[1m05|1M05]], [[1m6o|1M6O]], [[1mhe|1MHE]], [[1mi5|1MI5]], [[1n2r|1N2R]], [[1of2|1OF2]], [[1ogt|1OGT]], [[1onq|1ONQ]], [[1py4|1PY4]], [[1q94|1Q94]], [[1qlf|1QLF]], [[1qqd|1QQD]], [[1qvo|1QVO]], [[1r3h|1R3H]], [[1sys|1SYS]], [[1syv|1SYV]], [[1tmc|1TMC]], [[1uqs|1UQS]], [[1uxs|1UXS]], [[1uxw|1UXW]], [[1vgk|1VGK]], [[1w0v|1W0V]], [[1w0w|1W0W]], [[1w72|1W72]], [[1x7q|1X7Q]], [[1xh3|1XH3]], [[1xr8|1XR8]], [[1xr9|1XR9]], [[1xz0|1XZ0]], [[1ydp|1YDP]], [[1ypz|1YPZ]], [[1zs8|1ZS8]], [[1zsd|1ZSD]], [[1zt4|1ZT4]], [[2a83|2A83]], [[2ak4|2AK4]], [[2axf|2AXF]], [[2axg|2AXG]], [[2bck|2BCK]], [[2bsr|2BSR]], [[2bss|2BSS]], [[2bst|2BST]], [[2bvq|2BVQ]], [[2cii|2CII]], [[2cik|2CIK]], [[2d31|2D31]], [[2esv|2ESV]], [[2f74|2F74]], [[2f8o|2F8O]], [[2h26|2H26]], [[2hjk|2HJK]], [[2hjl|2HJL]], [[2hla|2HLA]], [[2v2w|2V2W]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2v2x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v2x OCA], [http://www.ebi.ac.uk/pdbsum/2v2x PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2v2x RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==Overview== | ||
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. | 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. | ||
| - | |||
| - | ==Disease== | ||
| - | Known diseases associated with this structure: Abacavir hypersensitivity, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=142800 142800]], Ankylosing spondylitis, susceptibility to, 1 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=142800 142800]], Hypoproteinemia, hypercatabolic OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=109700 109700]], Stevens-Johnson syndrome, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=142800 142800]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: ubl conjugation]] | [[Category: ubl conjugation]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:07:57 2008'' |
Revision as of 02:07, 31 March 2008
T CELL CROSS-REACTIVITY AND CONFORMATIONAL CHANGES DURING TCR ENGAGEMENT.
Overview
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.
About this Structure
2V2X is a Protein complex structure of sequences from Homo sapiens. This structure supersedes the now removed PDB entry 2BSV. Full crystallographic information is available from OCA.
Reference
T cell cross-reactivity and conformational changes during TCR engagement., Lee JK, Stewart-Jones G, Dong T, Harlos K, Di Gleria K, Dorrell L, Douek DC, van der Merwe PA, Jones EY, McMichael AJ, J Exp Med. 2004 Dec 6;200(11):1455-66. PMID:15583017
Page seeded by OCA on Mon Mar 31 05:07:57 2008
Categories: Homo sapiens | Protein complex | Dong, T. | Dorrell, L. | Douek, D C. | Gleria, K Di. | Harlos, K. | Jones, E Y. | Lee, J K. | Mcmichael, A J. | Merwe, P A.Van Der. | Stewart-Jones, G. | Disease mutation | Glycoprotein | Host-virus interaction | Immune response | Immune system | Immunoglobulin domain | Membrane | Mhc i | Mhc tcr hla-a2 hiv | Polymorphism | Pyrrolidone carboxylic acid | Transmembrane | Ubl conjugation
