4p2q: Difference between revisions
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<StructureSection load='4p2q' size='340' side='right' caption='[[4p2q]], [[Resolution|resolution]] 3.30Å' scene=''> | <StructureSection load='4p2q' size='340' side='right' caption='[[4p2q]], [[Resolution|resolution]] 3.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4p2q]] is a 20 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P2Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4P2Q FirstGlance]. <br> | <table><tr><td colspan='2'>[[4p2q]] is a 20 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice] and [http://en.wikipedia.org/wiki/Synthetic_construct_sequences Synthetic construct sequences]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P2Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4P2Q FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4p2o|4p2o]], [[4p2r|4p2r]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4p2o|4p2o]], [[4p2r|4p2r]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">H2-Eb1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4p2q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p2q OCA], [http://pdbe.org/4p2q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4p2q RCSB], [http://www.ebi.ac.uk/pdbsum/4p2q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4p2q ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4p2q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p2q OCA], [http://pdbe.org/4p2q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4p2q RCSB], [http://www.ebi.ac.uk/pdbsum/4p2q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4p2q ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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</div> | </div> | ||
<div class="pdbe-citations 4p2q" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 4p2q" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Lk3 transgenic mice]] | |||
[[Category: Synthetic construct sequences]] | |||
[[Category: Birnbaum, M E]] | [[Category: Birnbaum, M E]] | ||
[[Category: Garcia, K C]] | [[Category: Garcia, K C]] | ||
Revision as of 12:04, 1 November 2017
Crystal structure of the 5cc7 TCR in complex with 5c2/I-EkCrystal structure of the 5cc7 TCR in complex with 5c2/I-Ek
Structural highlights
Publication Abstract from PubMedIn 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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