4n5e

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'''Unreleased structure'''
 
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The entry 4n5e is ON HOLD until Paper Publication
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==42F3 TCR pCPA12/H-2Ld complex==
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<StructureSection load='4n5e' size='340' side='right'caption='[[4n5e]], [[Resolution|resolution]] 3.06&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4n5e]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4N5E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4N5E FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.059&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4n5e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n5e OCA], [https://pdbe.org/4n5e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4n5e RCSB], [https://www.ebi.ac.uk/pdbsum/4n5e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4n5e ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The T cell antigen receptor (TCR)-peptide-major histocompatibility complex (MHC) interface is composed of conserved and diverse regions, yet the relative contribution of each in shaping recognition by T cells remains unclear. Here we isolated cross-reactive peptides with limited homology, which allowed us to compare the structural properties of nine peptides for a single TCR-MHC pair. The TCR's cross-reactivity was rooted in highly similar recognition of an apical 'hot-spot' position in the peptide with tolerance of sequence variation at ancillary positions. Furthermore, we found a striking structural convergence onto a germline-mediated interaction between the TCR CDR1alpha region and the MHC alpha2 helix in twelve TCR-peptide-MHC complexes. Our studies suggest that TCR-MHC germline-mediated constraints, together with a focus on a small peptide hot spot, might place limits on peptide antigen cross-reactivity.
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Authors: Birnbaum, M.E., Adams, J.J., Garcia, K.C.
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Structural interplay between germline interactions and adaptive recognition determines the bandwidth of TCR-peptide-MHC cross-reactivity.,Adams JJ, Narayanan S, Birnbaum ME, Sidhu SS, Blevins SJ, Gee MH, Sibener LV, Baker BM, Kranz DM, Garcia KC Nat Immunol. 2016 Jan;17(1):87-94. doi: 10.1038/ni.3310. Epub 2015 Nov 2. PMID:26523866<ref>PMID:26523866</ref>
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Description: 42F3 TCR pCPA12/H-2Ld complex
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Garcia, K.C]]
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<div class="pdbe-citations 4n5e" style="background-color:#fffaf0;"></div>
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[[Category: Adams, J.J]]
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== References ==
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[[Category: Birnbaum, M.E]]
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Mus musculus]]
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[[Category: Adams JJ]]
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[[Category: Birnbaum ME]]
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[[Category: Garcia KC]]

Current revision

42F3 TCR pCPA12/H-2Ld complex

PDB ID 4n5e

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