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- | [[Image:2nx5.gif|left|200px]] | |
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- | {{Structure
| + | ==Crystal structure of ELS4 TCR bound to HLA-B*3501 presenting EBV peptide EPLPQGQLTAY at 1.7A== |
- | |PDB= 2nx5 |SIZE=350|CAPTION= <scene name='initialview01'>2nx5</scene>, resolution 2.700Å
| + | <StructureSection load='2nx5' size='340' side='right'caption='[[2nx5]], [[Resolution|resolution]] 2.70Å' scene=''> |
- | |SITE=
| + | == Structural highlights == |
- | |LIGAND=
| + | <table><tr><td colspan='2'>[[2nx5]] is a 20 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Human_herpesvirus_4_strain_B95-8 Human herpesvirus 4 strain B95-8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NX5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NX5 FirstGlance]. <br> |
- | |ACTIVITY=
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7Å</td></tr> |
- | |GENE=
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2nx5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nx5 OCA], [https://pdbe.org/2nx5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nx5 RCSB], [https://www.ebi.ac.uk/pdbsum/2nx5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nx5 ProSAT]</span></td></tr> |
- | |DOMAIN=
| + | </table> |
- | |RELATEDENTRY=
| + | == Function == |
- | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2nx5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nx5 OCA], [http://www.ebi.ac.uk/pdbsum/2nx5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2nx5 RCSB]</span>
| + | [https://www.uniprot.org/uniprot/BZLF1_EBVB9 BZLF1_EBVB9] Plays a key role in the switch from latent infection to lytic cycle producing new virions. Acts as a transcription factor, inducing early lytic cycle genes, and as a origin binding protein for genome replication. BZLF1 activates the promoter of another EBV gene (BSLF2+BMLF1).<ref>PMID:2157874</ref> <ref>PMID:1847997</ref> <ref>PMID:8404860</ref> <ref>PMID:17079287</ref> <ref>PMID:19144704</ref> |
- | }}
| + | == Evolutionary Conservation == |
| + | [[Image:Consurf_key_small.gif|200px|right]] |
| + | Check<jmol> |
| + | <jmolCheckbox> |
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nx/2nx5_consurf.spt"</scriptWhenChecked> |
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| + | <text>to colour the structure by Evolutionary Conservation</text> |
| + | </jmolCheckbox> |
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2nx5 ConSurf]. |
| + | <div style="clear:both"></div> |
| + | <div style="background-color:#fffaf0;"> |
| + | == Publication Abstract from PubMed == |
| + | Plasticity of the T cell receptor (TCR) is a hallmark of major histocompatibility complex (MHC)-restricted T cell recognition. However, it is unclear whether interactions of TCR and peptide-MHC class I (pMHCI) always conform to this paradigm. Here we describe the structure of a TCR, ELS4, in its non-ligand-bound form and in complex with a prominent 'bulged' Epstein-Barr virus peptide bound to HLA-B(*)3501. This complex was atypical of previously characterized TCR-pMHCI interactions in that a rigid face of the TCR crumpled the bulged antigenic determinant. This peptide 'bulldozing' created a more featureless pMHCI determinant, allowing the TCR to maximize MHC class I contacts essential for MHC class I restriction of TCR recognition. Our findings represent a mechanism of antigen recognition whereby the plasticity of the T cell response is dictated mainly by adjustments in the MHC-bound peptide. |
| | | |
- | '''Crystal structure of ELS4 TCR bound to HLA-B*3508 presenting EBV peptide EPLPQGQLTAY at 1.7A'''
| + | A T cell receptor flattens a bulged antigenic peptide presented by a major histocompatibility complex class I molecule.,Tynan FE, Reid HH, Kjer-Nielsen L, Miles JJ, Wilce MC, Kostenko L, Borg NA, Williamson NA, Beddoe T, Purcell AW, Burrows SR, McCluskey J, Rossjohn J Nat Immunol. 2007 Mar;8(3):268-76. Epub 2007 Jan 28. PMID:17259989<ref>PMID:17259989</ref> |
| | | |
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| + | </div> |
| + | <div class="pdbe-citations 2nx5" style="background-color:#fffaf0;"></div> |
| | | |
- | ==Overview== | + | ==See Also== |
- | Plasticity of the T cell receptor (TCR) is a hallmark of major histocompatibility complex (MHC)-restricted T cell recognition. However, it is unclear whether interactions of TCR and peptide-MHC class I (pMHCI) always conform to this paradigm. Here we describe the structure of a TCR, ELS4, in its non-ligand-bound form and in complex with a prominent 'bulged' Epstein-Barr virus peptide bound to HLA-B(*)3501. This complex was atypical of previously characterized TCR-pMHCI interactions in that a rigid face of the TCR crumpled the bulged antigenic determinant. This peptide 'bulldozing' created a more featureless pMHCI determinant, allowing the TCR to maximize MHC class I contacts essential for MHC class I restriction of TCR recognition. Our findings represent a mechanism of antigen recognition whereby the plasticity of the T cell response is dictated mainly by adjustments in the MHC-bound peptide.
| + | *[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]] |
- | | + | *[[T-cell receptor 3D structures|T-cell receptor 3D structures]] |
- | ==About this Structure==
| + | == References == |
- | 2NX5 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NX5 OCA].
| + | <references/> |
- | | + | __TOC__ |
- | ==Reference== | + | </StructureSection> |
- | A T cell receptor flattens a bulged antigenic peptide presented by a major histocompatibility complex class I molecule., Tynan FE, Reid HH, Kjer-Nielsen L, Miles JJ, Wilce MC, Kostenko L, Borg NA, Williamson NA, Beddoe T, Purcell AW, Burrows SR, McCluskey J, Rossjohn J, Nat Immunol. 2007 Mar;8(3):268-76. Epub 2007 Jan 28. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17259989 17259989]
| + | |
| [[Category: Homo sapiens]] | | [[Category: Homo sapiens]] |
- | [[Category: Protein complex]] | + | [[Category: Human herpesvirus 4 strain B95-8]] |
- | [[Category: Reid, H H.]] | + | [[Category: Large Structures]] |
- | [[Category: Rossjohn, J.]] | + | [[Category: Reid HH]] |
- | [[Category: Tynan, F E.]] | + | [[Category: Rossjohn J]] |
- | [[Category: immune complex]] | + | [[Category: Tynan FE]] |
- | [[Category: tcr-pmhc]]
| + | |
- | | + | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:09:36 2008''
| + | |
| Structural highlights
Function
BZLF1_EBVB9 Plays a key role in the switch from latent infection to lytic cycle producing new virions. Acts as a transcription factor, inducing early lytic cycle genes, and as a origin binding protein for genome replication. BZLF1 activates the promoter of another EBV gene (BSLF2+BMLF1).[1] [2] [3] [4] [5]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Plasticity of the T cell receptor (TCR) is a hallmark of major histocompatibility complex (MHC)-restricted T cell recognition. However, it is unclear whether interactions of TCR and peptide-MHC class I (pMHCI) always conform to this paradigm. Here we describe the structure of a TCR, ELS4, in its non-ligand-bound form and in complex with a prominent 'bulged' Epstein-Barr virus peptide bound to HLA-B(*)3501. This complex was atypical of previously characterized TCR-pMHCI interactions in that a rigid face of the TCR crumpled the bulged antigenic determinant. This peptide 'bulldozing' created a more featureless pMHCI determinant, allowing the TCR to maximize MHC class I contacts essential for MHC class I restriction of TCR recognition. Our findings represent a mechanism of antigen recognition whereby the plasticity of the T cell response is dictated mainly by adjustments in the MHC-bound peptide.
A T cell receptor flattens a bulged antigenic peptide presented by a major histocompatibility complex class I molecule.,Tynan FE, Reid HH, Kjer-Nielsen L, Miles JJ, Wilce MC, Kostenko L, Borg NA, Williamson NA, Beddoe T, Purcell AW, Burrows SR, McCluskey J, Rossjohn J Nat Immunol. 2007 Mar;8(3):268-76. Epub 2007 Jan 28. PMID:17259989[6]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Packham G, Economou A, Rooney CM, Rowe DT, Farrell PJ. Structure and function of the Epstein-Barr virus BZLF1 protein. J Virol. 1990 May;64(5):2110-6. PMID:2157874
- ↑ Kouzarides T, Packham G, Cook A, Farrell PJ. The BZLF1 protein of EBV has a coiled coil dimerisation domain without a heptad leucine repeat but with homology to the C/EBP leucine zipper. Oncogene. 1991 Feb;6(2):195-204. PMID:1847997
- ↑ Schepers A, Pich D, Hammerschmidt W. A transcription factor with homology to the AP-1 family links RNA transcription and DNA replication in the lytic cycle of Epstein-Barr virus. EMBO J. 1993 Oct;12(10):3921-9. PMID:8404860
- ↑ Wen W, Iwakiri D, Yamamoto K, Maruo S, Kanda T, Takada K. Epstein-Barr virus BZLF1 gene, a switch from latency to lytic infection, is expressed as an immediate-early gene after primary infection of B lymphocytes. J Virol. 2007 Jan;81(2):1037-42. Epub 2006 Nov 1. PMID:17079287 doi:10.1128/JVI.01416-06
- ↑ McDonald CM, Petosa C, Farrell PJ. Interaction of Epstein-Barr virus BZLF1 C-terminal tail structure and core zipper is required for DNA replication but not for promoter transactivation. J Virol. 2009 Apr;83(7):3397-401. doi: 10.1128/JVI.02500-08. Epub 2009 Jan 14. PMID:19144704 doi:10.1128/JVI.02500-08
- ↑ Tynan FE, Reid HH, Kjer-Nielsen L, Miles JJ, Wilce MC, Kostenko L, Borg NA, Williamson NA, Beddoe T, Purcell AW, Burrows SR, McCluskey J, Rossjohn J. A T cell receptor flattens a bulged antigenic peptide presented by a major histocompatibility complex class I molecule. Nat Immunol. 2007 Mar;8(3):268-76. Epub 2007 Jan 28. PMID:17259989 doi:10.1038/ni1432
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