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4p2o

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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4p2o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p2o OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4p2o RCSB], [http://www.ebi.ac.uk/pdbsum/4p2o PDBsum]</span></td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4p2o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p2o OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4p2o RCSB], [http://www.ebi.ac.uk/pdbsum/4p2o PDBsum]</span></td></tr>
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== Publication Abstract from PubMed ==
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In order to survey a universe of major histocompatibility complex (MHC)-presented peptide antigens whose numbers greatly exceed the diversity of the T cell repertoire, T cell receptors (TCRs) are thought to be cross-reactive. However, the nature and extent of TCR cross-reactivity has not been conclusively measured experimentally. We developed a system to identify MHC-presented peptide ligands by combining TCR selection of highly diverse yeast-displayed peptide-MHC libraries with deep sequencing. Although we identified hundreds of peptides reactive with each of five different mouse and human TCRs, the selected peptides possessed TCR recognition motifs that bore a close resemblance to their known antigens. This structural conservation of the TCR interaction surface allowed us to exploit deep-sequencing information to computationally identify activating microbial and self-ligands for human autoimmune TCRs. The mechanistic basis of TCR cross-reactivity described here enables effective surveillance of diverse self and foreign antigens without necessitating degenerate recognition of nonhomologous peptides.
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Deconstructing the Peptide-MHC Specificity of T Cell Recognition.,Birnbaum ME, Mendoza JL, Sethi DK, Dong S, Glanville J, Dobbins J, Ozkan E, Davis MM, Wucherpfennig KW, Garcia KC Cell. 2014 May 22;157(5):1073-87. doi: 10.1016/j.cell.2014.03.047. PMID:24855945<ref>PMID:24855945</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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== References ==
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<references/>
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</StructureSection>
</StructureSection>

Revision as of 06:17, 11 June 2014

Crystal structure of the 2B4 TCR in complex with 2A/I-Ek

4p2o, resolution 2.60Å

Drag the structure with the mouse to rotate

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