3rdt: Difference between revisions

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-'''Unreleased structure'''
-The entry 3rdt is ON HOLD
+==Crystal Structure of 809.B5 TCR complexed with MHC Class II I-Ab/3k peptide==
+<StructureSection load='3rdt' size='340' side='right'caption='[[3rdt]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[3rdt]] is a 4 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=3RDT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RDT 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]] 2.7&#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=3rdt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rdt OCA], [https://pdbe.org/3rdt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rdt RCSB], [https://www.ebi.ac.uk/pdbsum/3rdt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rdt ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/HA2B_MOUSE HA2B_MOUSE]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+A limited set of T cell receptor (TCR) variable (V) gene segments are used to create a repertoire of TCRs that recognize all major histocompatibility complex (MHC) ligands within a species. How individual alphabetaTCRs are constructed to specifically recognize a limited set of MHC ligands is unclear. Here we have identified a role for the differential pairing of particular V gene segments in creating TCRs that recognized MHC class II ligands exclusively, or cross-reacted with classical and nonclassical MHC class I ligands. Biophysical and structural experiments indicated that TCR specificity for MHC ligands is not driven by germline-encoded pairwise interactions. Rather, identical TCRbeta chains can have altered peptide-MHC (pMHC) binding modes when paired with different TCRalpha chains. The ability of TCR chain pairing to modify how V region residues interact with pMHC helps to explain how the same V genes are used to create TCRs specific for unique MHC ligands.
-Authors: Trenh, P., Huseby, E.S., Stern, L.J.
+A Role for Differential Variable Gene Pairing in Creating T Cell Receptors Specific for Unique Major Histocompatibility Ligands.,Stadinski BD, Trenh P, Smith RL, Bautista B, Huseby PG, Li G, Stern LJ, Huseby ES Immunity. 2011 Nov 16. PMID:22101158<ref>PMID:22101158</ref>
-Description: Crystal Structure of 809.B5 TCR complexed with MHC Class II I-Ab/3k peptide
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 3rdt" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[MHC 3D structures|MHC 3D structures]]
+*[[MHC II 3D structures|MHC II 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Mus musculus]]
+[[Category: Synthetic construct]]
+[[Category: Huseby ES]]
+[[Category: Stern LJ]]
+[[Category: Trenh P]]