3dx9

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{{Seed}}
 
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[[Image:3dx9.jpg|left|200px]]
 
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==Crystal Structure of the DM1 TCR at 2.75A==
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The line below this paragraph, containing "STRUCTURE_3dx9", creates the "Structure Box" on the page.
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<StructureSection load='3dx9' size='340' side='right'caption='[[3dx9]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3dx9]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DX9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DX9 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.75&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3dx9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dx9 OCA], [https://pdbe.org/3dx9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3dx9 RCSB], [https://www.ebi.ac.uk/pdbsum/3dx9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3dx9 ProSAT]</span></td></tr>
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{{STRUCTURE_3dx9| PDB=3dx9 | SCENE= }}
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</table>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dx/3dx9_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=3dx9 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Human leukocyte antigen (HLA) gene polymorphism plays a critical role in protective immunity, disease susceptibility, autoimmunity, and drug hypersensitivity, yet the basis of how HLA polymorphism influences T cell receptor (TCR) recognition is unclear. We examined how a natural micropolymorphism in HLA-B44, an important and large HLA allelic family, affected antigen recognition. T cell-mediated immunity to an Epstein-Barr virus determinant (EENLLDFVRF) is enhanced when HLA-B*4405 was the presenting allotype compared with HLA-B*4402 or HLA-B*4403, each of which differ by just one amino acid. The micropolymorphism in these HLA-B44 allotypes altered the mode of binding and dynamics of the bound viral epitope. The structure of the TCR-HLA-B*4405(EENLLDFVRF) complex revealed that peptide flexibility was a critical parameter in enabling preferential engagement with HLA-B*4405 in comparison to HLA-B*4402/03. Accordingly, major histocompatibility complex (MHC) polymorphism can alter the dynamics of the peptide-MHC landscape, resulting in fine-tuning of T cell responses between closely related allotypes.
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===Crystal Structure of the DM1 TCR at 2.75A===
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Natural micropolymorphism in human leukocyte antigens provides a basis for genetic control of antigen recognition.,Archbold JK, Macdonald WA, Gras S, Ely LK, Miles JJ, Bell MJ, Brennan RM, Beddoe T, Wilce MC, Clements CS, Purcell AW, McCluskey J, Burrows SR, Rossjohn J J Exp Med. 2009 Jan 16;206(1):209-19. Epub 2009 Jan 12. PMID:19139173<ref>PMID:19139173</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3dx9" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_19139173}}, adds the Publication Abstract to the page
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*[[T-cell receptor 3D structures|T-cell receptor 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 19139173 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_19139173}}
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__TOC__
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</StructureSection>
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==About this Structure==
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3DX9 is a 4 chains 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=3DX9 OCA].
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==Reference==
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<ref group="xtra">PMID:19139173</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Archbold, J K.]]
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[[Category: Large Structures]]
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[[Category: Gras, S.]]
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[[Category: Archbold JK]]
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[[Category: Macdonald, W A.]]
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[[Category: Gras S]]
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[[Category: Rossjohn, J.]]
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[[Category: Macdonald WA]]
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[[Category: Glycation]]
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[[Category: Rossjohn J]]
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[[Category: Glycoprotein]]
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[[Category: Host-virus interaction]]
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[[Category: Immune response]]
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[[Category: Immune system]]
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[[Category: Membrane]]
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[[Category: Mhc]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 28 09:46:50 2009''
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Current revision

Crystal Structure of the DM1 TCR at 2.75A

PDB ID 3dx9

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OCA

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