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| | <StructureSection load='4d0b' size='340' side='right'caption='[[4d0b]], [[Resolution|resolution]] 2.80Å' scene=''> | | <StructureSection load='4d0b' size='340' side='right'caption='[[4d0b]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4d0b]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Chick Chick]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2yf6 2yf6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D0B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4D0B FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4d0b]] 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=2yf6 2yf6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D0B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4D0B FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4d0c|4d0c]], [[4d0d|4d0d]]</td></tr> | + | </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=4d0b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d0b OCA], [https://pdbe.org/4d0b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4d0b RCSB], [https://www.ebi.ac.uk/pdbsum/4d0b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4d0b ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4d0b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d0b OCA], [http://pdbe.org/4d0b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4d0b RCSB], [http://www.ebi.ac.uk/pdbsum/4d0b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4d0b ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/B2MG_CHICK B2MG_CHICK]] Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system. | + | [[https://www.uniprot.org/uniprot/Q95601_CHICK Q95601_CHICK]] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Beta-2 microglobulin|Beta-2 microglobulin]] | + | *[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]] |
| - | *[[Major histocompatibility complex|Major histocompatibility complex]] | + | *[[MHC 3D structures|MHC 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Chick]] | + | [[Category: Gallus gallus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chappell, P E]] | + | [[Category: Chappell PE]] |
| - | [[Category: Harrison, M C]] | + | [[Category: Harrison MC]] |
| - | [[Category: Kaufman, J F]] | + | [[Category: Kaufman JF]] |
| - | [[Category: Lea, S M]] | + | [[Category: Lea SM]] |
| - | [[Category: Mears, L E]] | + | [[Category: Mears LE]] |
| - | [[Category: Roversi, P]] | + | [[Category: Roversi P]] |
| - | [[Category: Immune system]]
| + | |
| Structural highlights
Function
[Q95601_CHICK]
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ 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. Expression levels of MHC class I molecules are inversely correlated with promiscuity of peptide binding. Elife. 2015 Apr 10;4. doi: 10.7554/eLife.05345. PMID:25860507 doi:http://dx.doi.org/10.7554/eLife.05345
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