4n0c: Difference between revisions

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New page: '''Unreleased structure''' The entry 4n0c is ON HOLD Authors: Birnbaum, M.E., Adams, J.J., Garcia, K.C. Description: 42F3 TCR pCPE3/H-2Ld complex
 
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'''Unreleased structure'''


The entry 4n0c is ON HOLD
==42F3 TCR pCPE3/H-2Ld complex==
<StructureSection load='4n0c' size='340' side='right'caption='[[4n0c]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4n0c]] is a 8 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=4N0C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4N0C 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]] 2.9&#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=4n0c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n0c OCA], [https://pdbe.org/4n0c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4n0c RCSB], [https://www.ebi.ac.uk/pdbsum/4n0c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4n0c ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HA1L_MOUSE HA1L_MOUSE] Involved in the presentation of foreign antigens to the immune system.
<div style="background-color:#fffaf0;">
== 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.


Authors: Birnbaum, M.E., Adams, J.J., Garcia, K.C.
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>


Description: 42F3 TCR pCPE3/H-2Ld complex
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4n0c" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Adams JJ]]
[[Category: Birnbaum ME]]
[[Category: Garcia KC]]
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