7phr
From Proteopedia
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| - | ==== | + | ==Structure of a fully assembled T-cell receptor engaging a tumor-associated peptide-MHC I== |
| - | <StructureSection load='7phr' size='340' side='right'caption='[[7phr]]' scene=''> | + | <StructureSection load='7phr' size='340' side='right'caption='[[7phr]], [[Resolution|resolution]] 3.08Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7phr]] is a 11 chain structure with sequence from [https://en.wikipedia.org/wiki/Aequorea_victoria Aequorea victoria] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7PHR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PHR FirstGlance]. <br> |
| - | </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=7phr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7phr OCA], [https://pdbe.org/7phr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7phr RCSB], [https://www.ebi.ac.uk/pdbsum/7phr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7phr ProSAT]</span></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=7phr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7phr OCA], [https://pdbe.org/7phr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7phr RCSB], [https://www.ebi.ac.uk/pdbsum/7phr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7phr ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/CD3G_HUMAN CD3G_HUMAN]] The CD3 complex mediates signal transduction. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The T cell receptor (TCR) expressed by T lymphocytes initiates protective immune responses to pathogens and tumors. To explore the structural basis of how TCR signaling is initiated when the receptor binds to peptide-loaded major histocompatibility complex (pMHC) molecules, we used cryogenic electron microscopy to determine the structure of a tumor-reactive TCRalphabeta/CD3deltagammaepsilon2zeta2 complex bound to a melanoma-specific human class I pMHC at 3.08 A resolution. The antigen-bound complex comprises 11 subunits stabilized by multivalent interactions across three structural layers, with clustered membrane-proximal cystines stabilizing the CD3-epsilondelta and CD3-epsilongamma heterodimers. Extra density sandwiched between transmembrane helices reveals the involvement of sterol lipids in TCR assembly. The geometry of the pMHC/TCR complex suggests that efficient TCR scanning of pMHC requires accurate pre-positioning of T cell and antigen-presenting cell membranes. Comparisons of the ligand-bound and unliganded receptors, along with molecular dynamics simulations, indicate that TCRs can be triggered in the absence of spontaneous structural rearrangements. | ||
| + | |||
| + | Structure of a fully assembled tumor-specific T cell receptor ligated by pMHC.,Susac L, Vuong MT, Thomas C, von Bulow S, O'Brien-Ball C, Santos AM, Fernandes RA, Hummer G, Tampe R, Davis SJ Cell. 2022 Aug 18;185(17):3201-3213.e19. doi: 10.1016/j.cell.2022.07.010. PMID:35985289<ref>PMID:35985289</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7phr" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Aequorea victoria]] | ||
| + | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Susac L]] |
| + | [[Category: Tampe R]] | ||
| + | [[Category: Thomas C]] | ||
Revision as of 19:22, 7 September 2022
Structure of a fully assembled T-cell receptor engaging a tumor-associated peptide-MHC I
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