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| | ==42F3 TCR pCPA12/H-2Ld complex== | | ==42F3 TCR pCPA12/H-2Ld complex== |
| - | <StructureSection load='4n5e' size='340' side='right' caption='[[4n5e]], [[Resolution|resolution]] 3.06Å' scene=''> | + | <StructureSection load='4n5e' size='340' side='right'caption='[[4n5e]], [[Resolution|resolution]] 3.06Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4n5e]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] and [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4N5E FirstGlance]. <br> | + | <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> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3tf7|3tf7]], [[3tfk|3tfk]], [[3tjh|3tjh]], [[3tpu|3tpu]], [[4ms8|4ms8]], [[4mxq|4mxq]], [[4mvb|4mvb]], [[4n0c|4n0c]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.059Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">H2-L ([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'>[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> |
| - | <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=4n5e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n5e OCA], [http://pdbe.org/4n5e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4n5e RCSB], [http://www.ebi.ac.uk/pdbsum/4n5e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4n5e ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| - | == Function == | |
| - | [[http://www.uniprot.org/uniprot/HA1L_MOUSE HA1L_MOUSE]] Involved in the presentation of foreign antigens to the immune system. | |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Large Structures]] |
| - | [[Category: Adams, J J]] | + | [[Category: Mus musculus]] |
| - | [[Category: Birnbaum, M E]] | + | [[Category: Adams JJ]] |
| - | [[Category: Garcia, K C]] | + | [[Category: Birnbaum ME]] |
| - | [[Category: Antigen]] | + | [[Category: Garcia KC]] |
| - | [[Category: Ig]]
| + | |
| - | [[Category: Immune system]]
| + | |
| - | [[Category: Mhc]]
| + | |
| - | [[Category: Tcr]]
| + | |
| Structural highlights
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Adams JJ, Narayanan S, Birnbaum ME, Sidhu SS, Blevins SJ, Gee MH, Sibener LV, Baker BM, Kranz DM, Garcia KC. Structural interplay between germline interactions and adaptive recognition determines the bandwidth of TCR-peptide-MHC cross-reactivity. Nat Immunol. 2016 Jan;17(1):87-94. doi: 10.1038/ni.3310. Epub 2015 Nov 2. PMID:26523866 doi:http://dx.doi.org/10.1038/ni.3310
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