4p2q: Difference between revisions
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==Crystal structure of the 5cc7 TCR in complex with 5c2/I-Ek== | ==Crystal structure of the 5cc7 TCR in complex with 5c2/I-Ek== | ||
<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 [ | <table><tr><td colspan='2'>[[4p2q]] is a 20 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. 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 [https://proteopedia.org/fgij/fg.htm?mol=4P2Q FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.3Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4p2q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p2q OCA], [https://pdbe.org/4p2q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4p2q RCSB], [https://www.ebi.ac.uk/pdbsum/4p2q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4p2q ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/HA22_MOUSE HA22_MOUSE] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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==See Also== | ==See Also== | ||
*[[T-cell receptor|T-cell receptor]] | *[[T-cell receptor 3D structures|T-cell receptor 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Mus musculus]] | ||
[[Category: | [[Category: Synthetic construct]] | ||
[[Category: | [[Category: Birnbaum ME]] | ||
[[Category: | [[Category: Garcia KC]] | ||
[[Category: | [[Category: Ozkan E]] | ||
Latest revision as of 03:39, 28 December 2023
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
FunctionPublication 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. See AlsoReferences
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