5e8n: Difference between revisions
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==The structure of the TEIPP associated Trh4 peptide in complex with H-2D(b)== | ==The structure of the TEIPP associated Trh4 peptide in complex with H-2D(b)== | ||
<StructureSection load='5e8n' size='340' side='right' caption='[[5e8n]], [[Resolution|resolution]] 2.25Å' scene=''> | <StructureSection load='5e8n' size='340' side='right'caption='[[5e8n]], [[Resolution|resolution]] 2.25Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5e8n]] is a 12 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E8N OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[5e8n]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E8N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5E8N FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5e8n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e8n OCA], [https://pdbe.org/5e8n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5e8n RCSB], [https://www.ebi.ac.uk/pdbsum/5e8n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5e8n ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/CERS5_MOUSE CERS5_MOUSE] Dihydroceramide synthase. Catalyzes the acylation of sphingosine to form dihydroceramide, with high selectivity toward palmitoyl-CoA as acyl donor compared to stearoyl-CoA. Inhibited by fumonisin B1.<ref>PMID:12912983</ref> <ref>PMID:16100120</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 5e8n" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5e8n" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Achour | [[Category: Mus musculus]] | ||
[[Category: Buratto | [[Category: Achour A]] | ||
[[Category: Doorduijn | [[Category: Buratto J]] | ||
[[Category: Duru | [[Category: Doorduijn E]] | ||
[[Category: Hafstrand | [[Category: Duru AD]] | ||
[[Category: Hafstrand I]] | |||
[[Category: Oliveira | [[Category: Oliveira CC]] | ||
[[Category: Sandalova | [[Category: Sandalova T]] | ||
[[Category: | [[Category: Van Hall T]] | ||
Latest revision as of 07:01, 21 November 2024
The structure of the TEIPP associated Trh4 peptide in complex with H-2D(b)The structure of the TEIPP associated Trh4 peptide in complex with H-2D(b)
Structural highlights
FunctionCERS5_MOUSE Dihydroceramide synthase. Catalyzes the acylation of sphingosine to form dihydroceramide, with high selectivity toward palmitoyl-CoA as acyl donor compared to stearoyl-CoA. Inhibited by fumonisin B1.[1] [2] Publication Abstract from PubMedMHC class I downregulation represents a significant challenge for successful T cell-based immunotherapy. T cell epitopes associated with impaired peptide processing (TEIPP) constitute a novel category of immunogenic Ags that are selectively presented on transporter associated with Ag processing-deficient cells. The TEIPP neoepitopes are CD8 T cell targets, derived from nonmutated self-proteins that might be exploited to prevent immune escape. In this study, the crystal structure of H-2Db in complex with the first identified TEIPP Ag (MCLRMTAVM) derived from the Trh4 protein has been determined to 2.25 A resolution. In contrast to prototypic H-2Db peptides, Trh4 takes a noncanonical peptide-binding pattern with extensive sulfur-pi interactions that contribute to the overall complex stability. Importantly, the noncanonical methionine at peptide position 5 acts as a main anchor, altering only the conformation of the H-2Db residues Y156 and H155 and thereby forming a unique MHC/peptide conformer that is essential for recognition by TEIPP-specific T cells. Substitution of peptide residues p2C and p5M to the conservative alpha-aminobutyric acid and norleucine, respectively, significantly reduced complex stability, without altering peptide conformation or T cell recognition. In contrast, substitution of p5M to a conventional asparagine abolished recognition by the H-2Db/Trh4-specific T cell clone LnB5. We anticipate that the H-2Db/Trh4 complex represents the first example, to our knowledge, of a broader repertoire of alternative MHC class I binders. The MHC Class I Cancer-Associated Neoepitope Trh4 Linked with Impaired Peptide Processing Induces a Unique Noncanonical TCR Conformer.,Hafstrand I, Doorduijn EM, Duru AD, Buratto J, Oliveira CC, Sandalova T, van Hall T, Achour A J Immunol. 2016 Jan 22. pii: 1502249. PMID:26800871[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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