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3e3q

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{{Seed}}
 
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[[Image:3e3q.png|left|200px]]
 
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==Structure of the 3alpham13 high-affinity mutant of the 2C TCR in complex with Ld/QL9==
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The line below this paragraph, containing "STRUCTURE_3e3q", creates the "Structure Box" on the page.
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<StructureSection load='3e3q' size='340' side='right'caption='[[3e3q]], [[Resolution|resolution]] 2.95&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'>[[3e3q]] is a 32 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=3E3Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3E3Q 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]] 2.95&#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=3e3q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e3q OCA], [https://pdbe.org/3e3q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3e3q RCSB], [https://www.ebi.ac.uk/pdbsum/3e3q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3e3q ProSAT]</span></td></tr>
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{{STRUCTURE_3e3q| PDB=3e3q | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/HA1L_MOUSE HA1L_MOUSE] Involved in the presentation of foreign antigens to the immune system.
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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/e3/3e3q_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=3e3q 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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T cells are known to cross-react with diverse peptide MHC Ags through their alphabeta TCR. To explore the basis of such cross-reactivity, we examined the 2C TCR that recognizes two structurally distinct ligands, SIY-K(b) and alloantigen QL9-L(d). In this study we characterized the cross-reactivity of several high-affinity 2C TCR variants that contained mutations only in the CDR3alpha loop. Two of the TCR lost their ability to cross-react with the reciprocal ligand (SIY-K(b)), whereas another TCR (m67) maintained reactivity with both ligands. Crystal structures of four of the TCRs in complex with QL9-L(d) showed that CDR1, CDR2, and CDR3beta conformations and docking orientations were remarkably similar. Although the CDR3alpha loop of TCR m67 conferred a 2000-fold higher affinity for SIY-K(b), the TCR maintained the same docking angle on QL9-L(d) as the 2C TCR. Thus, CDR3alpha dictated the affinity and level of cross-reactivity, yet it did so without affecting the conserved docking orientation.
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===Structure of the 3alpham13 high-affinity mutant of the 2C TCR in complex with Ld/QL9===
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Distinct CDR3 conformations in TCRs determine the level of cross-reactivity for diverse antigens, but not the docking orientation.,Jones LL, Colf LA, Stone JD, Garcia KC, Kranz DM J Immunol. 2008 Nov 1;181(9):6255-64. PMID:18941216<ref>PMID:18941216</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 3e3q" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_18941216}}, adds the Publication Abstract to the page
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*[[MHC 3D structures|MHC 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 18941216 is the PubMed ID number.
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*[[MHC I 3D structures|MHC I 3D structures]]
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*[[T-cell receptor 3D structures|T-cell receptor 3D structures]]
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{{ABSTRACT_PUBMED_18941216}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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3E3Q is a 32 chains structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E3Q OCA].
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</StructureSection>
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[[Category: Large Structures]]
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==Reference==
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<ref group="xtra">PMID:18941216</ref><references group="xtra"/>
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Colf, L A.]]
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[[Category: Colf LA]]
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[[Category: Garcia, K C.]]
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[[Category: Garcia KC]]
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[[Category: Cross reactivity]]
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[[Category: Glycoprotein]]
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[[Category: High affinity]]
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[[Category: Immune response]]
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[[Category: Immune system]]
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[[Category: Immunoglobulin domain]]
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[[Category: Membrane]]
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[[Category: Mhc]]
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[[Category: Mhc i]]
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[[Category: Phosphoprotein]]
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[[Category: Receptor]]
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[[Category: Tcr]]
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[[Category: Transmembrane]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 07:44:37 2009''
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Current revision

Structure of the 3alpham13 high-affinity mutant of the 2C TCR in complex with Ld/QL9

PDB ID 3e3q

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