4d0c: Difference between revisions
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==COMPLEX OF A B21 CHICKEN MHC CLASS I MOLECULE AND A 10MER CHICKEN PEPTIDE== | |||
<StructureSection load='4d0c' size='340' side='right'caption='[[4d0c]], [[Resolution|resolution]] 2.81Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4d0c]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2yf5 2yf5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D0C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4D0C 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]] 2.81Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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=4d0c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d0c OCA], [https://pdbe.org/4d0c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4d0c RCSB], [https://www.ebi.ac.uk/pdbsum/4d0c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4d0c ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q95601_CHICK Q95601_CHICK] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Highly polymorphic MHC molecules are at the heart of adaptive immune responses, playing crucial roles in many kinds of disease and in vaccination. We report that breadth of peptide presentation and level of cell surface expression of class I molecules are inversely correlated in both chickens and humans. This relationship correlates with protective responses against infectious pathogens including Marek's disease virus leading to lethal tumours in chickens and HIV infection progressing to AIDS in humans. We propose that differences in peptide binding repertoire define two groups of MHC class I molecules strategically evolved as generalists and specialists for different modes of pathogen resistance. We suggest that differences in cell surface expression level ensure the development of optimal peripheral T cell responses. The inverse relationship of peptide repertoire and expression is evidently a fundamental property of MHC molecules, with ramifications extending beyond immunology and medicine to evolutionary biology and conservation. | |||
Expression levels of MHC class I molecules are inversely correlated with promiscuity of peptide binding.,Chappell P, Meziane EK, Harrison M, Magiera L, Hermann C, Mears L, Wrobel AG, Durant C, Nielsen LL, Buus S, Ternette N, Mwangi W, Butter C, Nair V, Ahyee T, Duggleby R, Madrigal A, Roversi P, Lea SM, Kaufman J Elife. 2015 Apr 10;4. doi: 10.7554/eLife.05345. PMID:25860507<ref>PMID:25860507</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Chappell | <div class="pdbe-citations 4d0c" style="background-color:#fffaf0;"></div> | ||
[[Category: Harrison | |||
[[Category: | ==See Also== | ||
[[Category: Lea | *[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]] | ||
[[Category: | *[[MHC 3D structures|MHC 3D structures]] | ||
[[Category: | *[[MHC I 3D structures|MHC I 3D structures]] | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Gallus gallus]] | |||
[[Category: Large Structures]] | |||
[[Category: Chappell PE]] | |||
[[Category: Harrison MC]] | |||
[[Category: Kaufman JF]] | |||
[[Category: Lea SM]] | |||
[[Category: Mears LE]] | |||
[[Category: Roversi P]] | |||
Latest revision as of 15:18, 20 December 2023
COMPLEX OF A B21 CHICKEN MHC CLASS I MOLECULE AND A 10MER CHICKEN PEPTIDECOMPLEX OF A B21 CHICKEN MHC CLASS I MOLECULE AND A 10MER CHICKEN PEPTIDE
Structural highlights
FunctionPublication Abstract from PubMedHighly polymorphic MHC molecules are at the heart of adaptive immune responses, playing crucial roles in many kinds of disease and in vaccination. We report that breadth of peptide presentation and level of cell surface expression of class I molecules are inversely correlated in both chickens and humans. This relationship correlates with protective responses against infectious pathogens including Marek's disease virus leading to lethal tumours in chickens and HIV infection progressing to AIDS in humans. We propose that differences in peptide binding repertoire define two groups of MHC class I molecules strategically evolved as generalists and specialists for different modes of pathogen resistance. We suggest that differences in cell surface expression level ensure the development of optimal peripheral T cell responses. The inverse relationship of peptide repertoire and expression is evidently a fundamental property of MHC molecules, with ramifications extending beyond immunology and medicine to evolutionary biology and conservation. Expression levels of MHC class I molecules are inversely correlated with promiscuity of peptide binding.,Chappell P, Meziane EK, Harrison M, Magiera L, Hermann C, Mears L, Wrobel AG, Durant C, Nielsen LL, Buus S, Ternette N, Mwangi W, Butter C, Nair V, Ahyee T, Duggleby R, Madrigal A, Roversi P, Lea SM, Kaufman J Elife. 2015 Apr 10;4. doi: 10.7554/eLife.05345. PMID:25860507[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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