5w1v: Difference between revisions
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==Structure of the HLA-E-VMAPRTLIL/GF4 TCR complex== | ==Structure of the HLA-E-VMAPRTLIL/GF4 TCR complex== | ||
<StructureSection load='5w1v' size='340' side='right' caption='[[5w1v]], [[Resolution|resolution]] 3.31Å' scene=''> | <StructureSection load='5w1v' size='340' side='right'caption='[[5w1v]], [[Resolution|resolution]] 3.31Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5w1v]] is a 20 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5W1V OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[5w1v]] is a 20 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Human_herpesvirus_5_strain_AD169 Human herpesvirus 5 strain AD169]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5W1V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5W1V 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]] 3.31Å</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=5w1v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5w1v OCA], [https://pdbe.org/5w1v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5w1v RCSB], [https://www.ebi.ac.uk/pdbsum/5w1v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5w1v ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/HLAE_HUMAN HLAE_HUMAN] Preferably binds to a peptide derived from the signal sequence of most HLA-A, -B, -C and -G molecules. | ||
<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 5w1v" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5w1v" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]] | |||
*[[T-cell receptor 3D structures|T-cell receptor 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Human herpesvirus 5 strain AD169]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Farenc C]] | ||
[[Category: | [[Category: Gras S]] | ||
[[Category: | [[Category: Rossjohn J]] | ||
[[Category: | [[Category: Walpole N]] | ||
Latest revision as of 15:17, 6 November 2024
Structure of the HLA-E-VMAPRTLIL/GF4 TCR complexStructure of the HLA-E-VMAPRTLIL/GF4 TCR complex
Structural highlights
FunctionHLAE_HUMAN Preferably binds to a peptide derived from the signal sequence of most HLA-A, -B, -C and -G molecules. Publication Abstract from PubMedalphabeta T cell receptors (TCRs) interact with peptides bound to the polymorphic Major Histocompatibility Complex class Ia (MHC-Ia) and class II (MHC-II) molecules, as well as the essentially monomorphic MHC class Ib (MHC-Ib) molecules. While there is a large amount of information on how TCRs engage with MHC-Ia and MHC-II, our understanding of TCR-MHC-Ib interactions is very limited. Infection with cytomegalovirus (CMV) can elicit a CD8+ T cell response restricted by the human MHC-Ib molecule, Human Leukocyte Antigen (HLA)-E, and specific for an epitope from UL40 (VMAPRTLIL), which is characterized by biased TRBV14 gene usage. Here we describe an HLA-E-restricted CD8+ T cell able to recognize an allotypic variant of the UL40 peptide, with a modification at position 8 (P8) of the peptide (VMAPRTLVL) that uses the TRBV9 gene segment. We report the structures of a TRBV9+ TCR in complex with the HLA-E molecule presenting the two peptides. Our data revealed that the TRBV9+ TCR adopts a different docking mode and molecular footprint atop HLA-E when compared with the TRBV14+ TCR-HLA-E ternary complex. Additionally, despite their differing V gene segment usage and different docking mechanisms, mutational analyses showed that the TCRs shared a conserved energetic footprint on the HLA-E molecule, focussed around the peptide-binding groove. Hence, we provide new insights into how monomorphic MHC molecules interact with T cells. A conserved energetic footprint underpins recognition of Human Leukocyte Antigen-E by two distinct alphabeta T cell receptors.,Sullivan LC, Walpole NG, Farenc C, Pietra G, Sum MJW, Clements CS, Lee EJ, Beddoe T, Falco M, Mingari MC, Moretta L, Gras S, Rossjohn J, Brooks AG J Biol Chem. 2017 Sep 25. pii: jbc.M117.807719. doi: 10.1074/jbc.M117.807719. PMID:28972140[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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