7jwj: Difference between revisions
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==Crystal Structure of B17-C1 TCR-H2Db== | |||
<StructureSection load='7jwj' size='340' side='right'caption='[[7jwj]], [[Resolution|resolution]] 3.25Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7jwj]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_A_virus Influenza A virus] 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=7JWJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7JWJ 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]] 3.251Å</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=7jwj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7jwj OCA], [https://pdbe.org/7jwj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7jwj RCSB], [https://www.ebi.ac.uk/pdbsum/7jwj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7jwj 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 == | |||
T cell receptor (TCR) recognition of peptide-major histocompatibility complexes (pMHCs) is characterized by a highly conserved docking polarity. Whether this polarity is driven by recognition or signaling constraints remains unclear. Using "reversed-docking" TCRbeta-variable (TRBV) 17(+) TCRs from the naive mouse CD8(+) T cell repertoire that recognizes the H-2D(b)-NP(366) epitope, we demonstrate that their inability to support T cell activation and in vivo recruitment is a direct consequence of reversed docking polarity and not TCR-pMHCI binding or clustering characteristics. Canonical TCR-pMHCI docking optimally localizes CD8/Lck to the CD3 complex, which is prevented by reversed TCR-pMHCI polarity. The requirement for canonical docking was circumvented by dissociating Lck from CD8. Thus, the consensus TCR-pMHC docking topology is mandated by T cell signaling constraints. | |||
Canonical T cell receptor docking on peptide-MHC is essential for T cell signaling.,Zareie P, Szeto C, Farenc C, Gunasinghe SD, Kolawole EM, Nguyen A, Blyth C, Sng XYX, Li J, Jones CM, Fulcher AJ, Jacobs JR, Wei Q, Wojciech L, Petersen J, Gascoigne NRJ, Evavold BD, Gaus K, Gras S, Rossjohn J, La Gruta NL Science. 2021 Jun 4;372(6546):eabe9124. doi: 10.1126/science.abe9124. PMID:34083463<ref>PMID:34083463</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 7jwj" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Influenza A virus]] | |||
[[Category: Large Structures]] | |||
[[Category: Mus musculus]] | |||
[[Category: Farenc C]] | |||
[[Category: Gras S]] | |||
[[Category: Rossjohn J]] | |||
[[Category: Szeto C]] | |||
Latest revision as of 18:12, 18 October 2023
Crystal Structure of B17-C1 TCR-H2DbCrystal Structure of B17-C1 TCR-H2Db
Structural highlights
FunctionHA11_MOUSE Involved in the presentation of foreign antigens to the immune system. Publication Abstract from PubMedT cell receptor (TCR) recognition of peptide-major histocompatibility complexes (pMHCs) is characterized by a highly conserved docking polarity. Whether this polarity is driven by recognition or signaling constraints remains unclear. Using "reversed-docking" TCRbeta-variable (TRBV) 17(+) TCRs from the naive mouse CD8(+) T cell repertoire that recognizes the H-2D(b)-NP(366) epitope, we demonstrate that their inability to support T cell activation and in vivo recruitment is a direct consequence of reversed docking polarity and not TCR-pMHCI binding or clustering characteristics. Canonical TCR-pMHCI docking optimally localizes CD8/Lck to the CD3 complex, which is prevented by reversed TCR-pMHCI polarity. The requirement for canonical docking was circumvented by dissociating Lck from CD8. Thus, the consensus TCR-pMHC docking topology is mandated by T cell signaling constraints. Canonical T cell receptor docking on peptide-MHC is essential for T cell signaling.,Zareie P, Szeto C, Farenc C, Gunasinghe SD, Kolawole EM, Nguyen A, Blyth C, Sng XYX, Li J, Jones CM, Fulcher AJ, Jacobs JR, Wei Q, Wojciech L, Petersen J, Gascoigne NRJ, Evavold BD, Gaus K, Gras S, Rossjohn J, La Gruta NL Science. 2021 Jun 4;372(6546):eabe9124. doi: 10.1126/science.abe9124. PMID:34083463[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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