3e2h: Difference between revisions

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{{Seed}}
[[Image:3e2h.jpg|left|200px]]


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==Structure of the m67 high-affinity mutant of the 2C TCR in complex with Ld/QL9==
The line below this paragraph, containing "STRUCTURE_3e2h", creates the "Structure Box" on the page.
<StructureSection load='3e2h' size='340' side='right'caption='[[3e2h]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[3e2h]] 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=3E2H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3E2H FirstGlance]. <br>
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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]] 3.8&#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=3e2h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e2h OCA], [https://pdbe.org/3e2h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3e2h RCSB], [https://www.ebi.ac.uk/pdbsum/3e2h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3e2h ProSAT]</span></td></tr>
{{STRUCTURE_3e2h|  PDB=3e2h  |  SCENE=  }}
</table>
== Function ==
[https://www.uniprot.org/uniprot/HA1L_MOUSE HA1L_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/e2/3e2h_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=3e2h ConSurf].
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== Publication Abstract from PubMed ==
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.


===Structure of the m67 high-affinity mutant of the 2C TCR in complex with Ld/QL9===
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>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3e2h" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_18941216}}, adds the Publication Abstract to the page
*[[MHC 3D structures|MHC 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 18941216 is the PubMed ID number.
*[[MHC I 3D structures|MHC I 3D structures]]
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*[[T-cell receptor 3D structures|T-cell receptor 3D structures]]
{{ABSTRACT_PUBMED_18941216}}
== References ==
 
<references/>
==About this Structure==
__TOC__
3E2H is a [[Protein complex]] 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=3E2H OCA].
</StructureSection>
 
[[Category: Large Structures]]
==Reference==
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:[http://www.ncbi.nlm.nih.gov/pubmed/18941216 18941216]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Protein complex]]
[[Category: Colf LA]]
[[Category: Colf, L A.]]
[[Category: Garcia KC]]
[[Category: Garcia, K C.]]
[[Category: Cross-reactivity]]
[[Category: Glycoprotein]]
[[Category: High affinity]]
[[Category: Immune response]]
[[Category: Immune system]]
[[Category: Immunoglobulin domain]]
[[Category: Membrane]]
[[Category: Mhc]]
[[Category: Mhc i]]
[[Category: Phosphoprotein]]
[[Category: Receptor]]
[[Category: Tcr]]
[[Category: Transmembrane]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Nov  5 12:51:19 2008''

Latest revision as of 05:46, 17 October 2024

Structure of the m67 high-affinity mutant of the 2C TCR in complex with Ld/QL9

3e2h, resolution 3.80Å

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