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[[Image:2p1y.jpg|left|200px]]
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{{STRUCTURE_2p1y|  PDB=2p1y  |  SCENE=  }}
'''1.B2.D9, a bispecific alpha/beta TCR'''


==1.B2.D9, a bispecific alpha/beta TCR==
<StructureSection load='2p1y' size='340' side='right'caption='[[2p1y]], [[Resolution|resolution]] 2.42&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2p1y]] 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=2P1Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2P1Y 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]] 2.42&#8491;</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=2p1y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p1y OCA], [https://pdbe.org/2p1y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2p1y RCSB], [https://www.ebi.ac.uk/pdbsum/2p1y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2p1y ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q5R1B3_MOUSE Q5R1B3_MOUSE]
== 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/p1/2p1y_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=2p1y ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
We report crystal structures of a negatively selected T cell receptor (TCR) that recognizes two I-A(u)-restricted myelin basic protein peptides and one of its peptide/major histocompatibility complex (pMHC) ligands. Unusual complementarity-determining region (CDR) structural features revealed by our analyses identify a previously unrecognized mechanism by which the highly variable CDR3 regions define ligand specificity. In addition to the pMHC contact residues contributed by CDR3, the CDR3 residues buried deep within the V alpha/V beta interface exert indirect effects on recognition by influencing the V alpha/V beta interdomain angle. This phenomenon represents an additional mechanism for increasing the potential diversity of the TCR repertoire. Both the direct and indirect effects exerted by CDR residues can impact global TCR/MHC docking. Analysis of the available TCR structures in light of these results highlights the significance of the V alpha/V beta interdomain angle in determining specificity and indicates that TCR/pMHC interface features do not distinguish autoimmune from non-autoimmune class II-restricted TCRs.


==Overview==
A new twist in TCR diversity revealed by a forbidden alphabeta TCR.,McBeth C, Seamons A, Pizarro JC, Fleishman SJ, Baker D, Kortemme T, Goverman JM, Strong RK J Mol Biol. 2008 Feb 1;375(5):1306-19. Epub 2007 Nov 17. PMID:18155234<ref>PMID:18155234</ref>
We report crystal structures of a negatively selected T cell receptor (TCR) that recognizes two I-A(u)-restricted myelin basic protein peptides and one of its peptide/major histocompatibility complex (pMHC) ligands. Unusual complementarity-determining region (CDR) structural features revealed by our analyses identify a previously unrecognized mechanism by which the highly variable CDR3 regions define ligand specificity. In addition to the pMHC contact residues contributed by CDR3, the CDR3 residues buried deep within the V alpha/V beta interface exert indirect effects on recognition by influencing the V alpha/V beta interdomain angle. This phenomenon represents an additional mechanism for increasing the potential diversity of the TCR repertoire. Both the direct and indirect effects exerted by CDR residues can impact global TCR/MHC docking. Analysis of the available TCR structures in light of these results highlights the significance of the V alpha/V beta interdomain angle in determining specificity and indicates that TCR/pMHC interface features do not distinguish autoimmune from non-autoimmune class II-restricted TCRs.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
2P1Y is a [[Single protein]] structure of sequence 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=2P1Y OCA].
</div>
<div class="pdbe-citations 2p1y" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
A new twist in TCR diversity revealed by a forbidden alphabeta TCR., McBeth C, Seamons A, Pizarro JC, Fleishman SJ, Baker D, Kortemme T, Goverman JM, Strong RK, J Mol Biol. 2008 Feb 1;375(5):1306-19. Epub 2007 Nov 17. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18155234 18155234]
*[[T-cell receptor 3D structures|T-cell receptor 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: McBeth C]]
[[Category: McBeth, C.]]
[[Category: Pizarro JC]]
[[Category: Pizarro, J C.]]
[[Category: Strong RK]]
[[Category: Strong, R K.]]
[[Category: Autoimmunity]]
[[Category: Diabody]]
[[Category: Immune system]]
[[Category: Immunoglobulin fold]]
[[Category: Tcr]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 12:10:19 2008''

Latest revision as of 01:18, 21 November 2024

1.B2.D9, a bispecific alpha/beta TCR

2p1y, resolution 2.42Å

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