2xfx: Difference between revisions
New page: '''Unreleased structure''' The entry 2xfx is ON HOLD Authors: Macdonald, I.K., Harkiolaki, M., Hunt, L., Morrison, W.I., Connelley, T., Graham, S.P., Jones, E.Y., Flower, D.R., Ellis, S... |
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The | ==cattle MHC class I N01301 presenting an 11mer from Theileria parva== | ||
<StructureSection load='2xfx' size='340' side='right'caption='[[2xfx]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2xfx]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [https://en.wikipedia.org/wiki/Theileria_parva Theileria parva]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XFX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XFX 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]] 1.9Å</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=2xfx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xfx OCA], [https://pdbe.org/2xfx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xfx RCSB], [https://www.ebi.ac.uk/pdbsum/2xfx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xfx ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q30291_BOVIN Q30291_BOVIN] Involved in the presentation of foreign antigens to the immune system.[SAAS:SAAS00004076] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
T cell receptor (TCR) recognition of peptide-MHC class I (pMHC) complexes is a crucial event in the adaptive immune response to pathogens. Peptide epitopes often display a strong dominance hierarchy, resulting in focusing of the response on a limited number of the most dominant epitopes. Such T cell responses may be additionally restricted by particular MHC alleles in preference to others. We have studied this poorly understood phenomenon using Theileria parva, a protozoan parasite that causes an often fatal lymphoproliferative disease in cattle. Despite its antigenic complexity, CD8+ T cell responses induced by infection with the parasite show profound immunodominance, as exemplified by the Tp1(214-224) epitope presented by the common and functionally important MHC class I allele N*01301. We present a high-resolution crystal structure of this pMHC complex, demonstrating that the peptide is presented in a distinctive raised conformation. Functional studies using CD8+ T cell clones show that this impacts significantly on TCR recognition. The unconventional structure is generated by a hydrophobic ridge within the MHC peptide binding groove, found in a set of cattle MHC alleles. Extremely rare in all other species, this feature is seen in a small group of mouse MHC class I molecules. The data generated in this analysis contribute to our understanding of the structural basis for T cell-dependent immune responses, providing insight into what determines a highly immunogenic p-MHC complex, and hence can be of value in prediction of antigenic epitopes and vaccine design. | |||
MHC class I bound to an immunodominant Theileria parva epitope demonstrates unconventional presentation to T cell receptors.,Macdonald IK, Harkiolaki M, Hunt L, Connelley T, Carroll AV, MacHugh ND, Graham SP, Jones EY, Morrison WI, Flower DR, Ellis SA PLoS Pathog. 2010 Oct 14;6(10):e1001149. PMID:20976198<ref>PMID:20976198</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2xfx" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bos taurus]] | |||
[[Category: Large Structures]] | |||
[[Category: Theileria parva]] | |||
[[Category: Connelley T]] | |||
[[Category: Ellis SA]] | |||
[[Category: Flower DR]] | |||
[[Category: Graham SP]] | |||
[[Category: Harkiolaki M]] | |||
[[Category: Hunt L]] | |||
[[Category: Jones EY]] | |||
[[Category: Macdonald IK]] | |||
[[Category: Morrison WI]] | |||
Latest revision as of 13:38, 16 August 2023
cattle MHC class I N01301 presenting an 11mer from Theileria parvacattle MHC class I N01301 presenting an 11mer from Theileria parva
Structural highlights
FunctionQ30291_BOVIN Involved in the presentation of foreign antigens to the immune system.[SAAS:SAAS00004076] Publication Abstract from PubMedT cell receptor (TCR) recognition of peptide-MHC class I (pMHC) complexes is a crucial event in the adaptive immune response to pathogens. Peptide epitopes often display a strong dominance hierarchy, resulting in focusing of the response on a limited number of the most dominant epitopes. Such T cell responses may be additionally restricted by particular MHC alleles in preference to others. We have studied this poorly understood phenomenon using Theileria parva, a protozoan parasite that causes an often fatal lymphoproliferative disease in cattle. Despite its antigenic complexity, CD8+ T cell responses induced by infection with the parasite show profound immunodominance, as exemplified by the Tp1(214-224) epitope presented by the common and functionally important MHC class I allele N*01301. We present a high-resolution crystal structure of this pMHC complex, demonstrating that the peptide is presented in a distinctive raised conformation. Functional studies using CD8+ T cell clones show that this impacts significantly on TCR recognition. The unconventional structure is generated by a hydrophobic ridge within the MHC peptide binding groove, found in a set of cattle MHC alleles. Extremely rare in all other species, this feature is seen in a small group of mouse MHC class I molecules. The data generated in this analysis contribute to our understanding of the structural basis for T cell-dependent immune responses, providing insight into what determines a highly immunogenic p-MHC complex, and hence can be of value in prediction of antigenic epitopes and vaccine design. MHC class I bound to an immunodominant Theileria parva epitope demonstrates unconventional presentation to T cell receptors.,Macdonald IK, Harkiolaki M, Hunt L, Connelley T, Carroll AV, MacHugh ND, Graham SP, Jones EY, Morrison WI, Flower DR, Ellis SA PLoS Pathog. 2010 Oct 14;6(10):e1001149. PMID:20976198[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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