2xfx: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
 
(5 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:2xfx.png|left|200px]]


{{STRUCTURE_2xfx| PDB=2xfx | SCENE= }}
==cattle MHC class I N01301 presenting an 11mer from Theileria parva==
<StructureSection load='2xfx' size='340' side='right'caption='[[2xfx]], [[Resolution|resolution]] 1.90&Aring;' 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]] 1.9&#8491;</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.


===cattle MHC class I N01301 presenting an 11mer from Theileria parva===
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>


{{ABSTRACT_PUBMED_20976198}}
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
==About this Structure==
<div class="pdbe-citations 2xfx" style="background-color:#fffaf0;"></div>
[[2xfx]] is a 3 chain structure of [[Beta-2 microglobulin]] with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://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].


==See Also==
==See Also==
*[[Beta-2 microglobulin|Beta-2 microglobulin]]
*[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:020976198</ref><references group="xtra"/>
__TOC__
</StructureSection>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Large Structures]]
[[Category: Theileria parva]]
[[Category: Theileria parva]]
[[Category: Connelley, T.]]
[[Category: Connelley T]]
[[Category: Ellis, S A.]]
[[Category: Ellis SA]]
[[Category: Flower, D R.]]
[[Category: Flower DR]]
[[Category: Graham, S P.]]
[[Category: Graham SP]]
[[Category: Harkiolaki, M.]]
[[Category: Harkiolaki M]]
[[Category: Hunt, L.]]
[[Category: Hunt L]]
[[Category: Jones, E Y.]]
[[Category: Jones EY]]
[[Category: Macdonald, I K.]]
[[Category: Macdonald IK]]
[[Category: Morrison, W I.]]
[[Category: Morrison WI]]
[[Category: East coast fever]]
[[Category: Immune system]]
[[Category: Major histocompatibility]]
[[Category: Theileriosis]]
Retrieved from "https://proteopedia.org/2xfx"