1nez
From Proteopedia
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- | [[Image:1nez.jpg|left|200px]] | ||
- | + | ==The Crystal Structure of a TL/CD8aa Complex at 2.1A resolution:Implications for Memory T cell Generation, Co-receptor Preference and Affinity== | |
- | + | <StructureSection load='1nez' size='340' side='right'caption='[[1nez]], [[Resolution|resolution]] 2.10Å' scene=''> | |
- | + | == Structural highlights == | |
- | | | + | <table><tr><td colspan='2'>[[1nez]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NEZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NEZ FirstGlance]. <br> |
- | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> | |
- | | | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> |
- | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1nez FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nez OCA], [https://pdbe.org/1nez PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nez RCSB], [https://www.ebi.ac.uk/pdbsum/1nez PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nez ProSAT]</span></td></tr> | |
- | + | </table> | |
- | + | == Function == | |
- | + | [https://www.uniprot.org/uniprot/HA1T_MOUSE HA1T_MOUSE] Involved in the presentation of foreign antigens to the immune system. | |
- | + | == 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/ne/1nez_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=1nez ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
TL is a nonclassical MHC class I molecule that modulates T cell activation through relatively high-affinity interaction with CD8alphaalpha. To investigate how the TL/CD8alphaalpha interaction influences TCR signaling, we characterized the structure of the TL/CD8alphaalpha complex using X-ray crystallography. Unlike antigen-presenting molecules, the TL antigen-binding groove is occluded by specific conformational changes. This feature eliminates antigen presentation, severely hampers direct TCR recognition, and prevents TL from participating in the TCR activation complex. At the same time, the TL/CD8alphaalpha interaction is strengthened through subtle structure changes in the TL alpha3 domain. Thus, TL functions to sequester and redirect CD8alphaalpha away from the TCR, modifying lck-dependent signaling. | TL is a nonclassical MHC class I molecule that modulates T cell activation through relatively high-affinity interaction with CD8alphaalpha. To investigate how the TL/CD8alphaalpha interaction influences TCR signaling, we characterized the structure of the TL/CD8alphaalpha complex using X-ray crystallography. Unlike antigen-presenting molecules, the TL antigen-binding groove is occluded by specific conformational changes. This feature eliminates antigen presentation, severely hampers direct TCR recognition, and prevents TL from participating in the TCR activation complex. At the same time, the TL/CD8alphaalpha interaction is strengthened through subtle structure changes in the TL alpha3 domain. Thus, TL functions to sequester and redirect CD8alphaalpha away from the TCR, modifying lck-dependent signaling. | ||
- | + | The crystal structure of a TL/CD8alphaalpha complex at 2.1 A resolution: implications for modulation of T cell activation and memory.,Liu Y, Xiong Y, Naidenko OV, Liu JH, Zhang R, Joachimiak A, Kronenberg M, Cheroutre H, Reinherz EL, Wang JH Immunity. 2003 Feb;18(2):205-15. PMID:12594948<ref>PMID:12594948</ref> | |
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- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | <div class="pdbe-citations 1nez" style="background-color:#fffaf0;"></div> | |
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- | + | ==See Also== | |
+ | *[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]] | ||
+ | *[[CD8 3D structures|CD8 3D structures]] | ||
+ | *[[MHC 3D structures|MHC 3D structures]] | ||
+ | *[[MHC I 3D structures|MHC I 3D structures]] | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Mus musculus]] | ||
+ | [[Category: Cheroutre H]] | ||
+ | [[Category: Joachimiak A]] | ||
+ | [[Category: Kronenberg M]] | ||
+ | [[Category: Liu JH]] | ||
+ | [[Category: Liu Y]] | ||
+ | [[Category: Naidenko OV]] | ||
+ | [[Category: Reinherz EL]] | ||
+ | [[Category: Wang JH]] | ||
+ | [[Category: Xiong Y]] | ||
+ | [[Category: Zhang R]] |
Current revision
The Crystal Structure of a TL/CD8aa Complex at 2.1A resolution:Implications for Memory T cell Generation, Co-receptor Preference and Affinity
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Categories: Large Structures | Mus musculus | Cheroutre H | Joachimiak A | Kronenberg M | Liu JH | Liu Y | Naidenko OV | Reinherz EL | Wang JH | Xiong Y | Zhang R