5sws: Difference between revisions

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New page: '''Unreleased structure''' The entry 5sws is ON HOLD until Paper Publication Authors: Description: Category: Unreleased Structures
 
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'''Unreleased structure'''


The entry 5sws is ON HOLD  until Paper Publication
==Crystal Structure of NP2-B17 TCR-H2Db-NP complex==
<StructureSection load='5sws' size='340' side='right'caption='[[5sws]], [[Resolution|resolution]] 2.86&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5sws]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Unidentified_influenza_virus Unidentified influenza virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5SWS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5SWS 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]] 2.86&#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=5sws FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5sws OCA], [https://pdbe.org/5sws PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5sws RCSB], [https://www.ebi.ac.uk/pdbsum/5sws PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5sws ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HA11_MOUSE HA11_MOUSE] Involved in the presentation of foreign antigens to the immune system.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The anti-viral T cell response is drawn from the naive T cell repertoire. During influenza infection, the CD8+ T cell response to an H-2Db-restricted nucleoprotein epitope (NP366) is characterized by preferential expansion of T cells bearing TRBV13+ T cell receptors (TCRs) and avoidance of TRBV17+ T cells, despite the latter dominating the naive precursor repertoire. We found two TRBV17+ TCRs that bound H-2Db-NP366 with a 180 degrees reversed polarity compared to the canonical TCR-pMHC-I docking. The TRBV17 beta-chain dominated the interaction and, whereas the complementarity determining region-3 (CDR3) loops exclusively mediated contacts with the MHC-I, peptide specificity was attributable to germline-encoded recognition. Nevertheless, the TRBV17+ TCR exhibited moderate affinity toward H-2Db-NP366 and was capable of signal transduction. Thus, the naive CD8+ T cell pool can comprise TCRs adopting reversed pMHC-I docking modes that limit their involvement in the immune response.


Authors:  
Reversed T Cell Receptor Docking on a Major Histocompatibility Class I Complex Limits Involvement in the Immune Response.,Gras S, Chadderton J, Del Campo CM, Farenc C, Wiede F, Josephs TM, Sng XY, Mirams M, Watson KA, Tiganis T, Quinn KM, Rossjohn J, La Gruta NL Immunity. 2016 Oct 18;45(4):749-760. doi: 10.1016/j.immuni.2016.09.007. Epub 2016, Oct 4. PMID:27717799<ref>PMID:27717799</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 5sws" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Unidentified influenza virus]]
[[Category: Del Campo CM]]
[[Category: Farenc C]]
[[Category: Gras S]]
[[Category: Josephs TM]]
[[Category: Rossjohn J]]

Latest revision as of 15:49, 4 October 2023

Crystal Structure of NP2-B17 TCR-H2Db-NP complexCrystal Structure of NP2-B17 TCR-H2Db-NP complex

Structural highlights

5sws is a 5 chain structure with sequence from Mus musculus and Unidentified influenza virus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.86Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

HA11_MOUSE Involved in the presentation of foreign antigens to the immune system.

Publication Abstract from PubMed

The anti-viral T cell response is drawn from the naive T cell repertoire. During influenza infection, the CD8+ T cell response to an H-2Db-restricted nucleoprotein epitope (NP366) is characterized by preferential expansion of T cells bearing TRBV13+ T cell receptors (TCRs) and avoidance of TRBV17+ T cells, despite the latter dominating the naive precursor repertoire. We found two TRBV17+ TCRs that bound H-2Db-NP366 with a 180 degrees reversed polarity compared to the canonical TCR-pMHC-I docking. The TRBV17 beta-chain dominated the interaction and, whereas the complementarity determining region-3 (CDR3) loops exclusively mediated contacts with the MHC-I, peptide specificity was attributable to germline-encoded recognition. Nevertheless, the TRBV17+ TCR exhibited moderate affinity toward H-2Db-NP366 and was capable of signal transduction. Thus, the naive CD8+ T cell pool can comprise TCRs adopting reversed pMHC-I docking modes that limit their involvement in the immune response.

Reversed T Cell Receptor Docking on a Major Histocompatibility Class I Complex Limits Involvement in the Immune Response.,Gras S, Chadderton J, Del Campo CM, Farenc C, Wiede F, Josephs TM, Sng XY, Mirams M, Watson KA, Tiganis T, Quinn KM, Rossjohn J, La Gruta NL Immunity. 2016 Oct 18;45(4):749-760. doi: 10.1016/j.immuni.2016.09.007. Epub 2016, Oct 4. PMID:27717799[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Gras S, Chadderton J, Del Campo CM, Farenc C, Wiede F, Josephs TM, Sng XY, Mirams M, Watson KA, Tiganis T, Quinn KM, Rossjohn J, La Gruta NL. Reversed T Cell Receptor Docking on a Major Histocompatibility Class I Complex Limits Involvement in the Immune Response. Immunity. 2016 Oct 18;45(4):749-760. doi: 10.1016/j.immuni.2016.09.007. Epub 2016, Oct 4. PMID:27717799 doi:http://dx.doi.org/10.1016/j.immuni.2016.09.007

5sws, resolution 2.86Å

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