2yez: Difference between revisions

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[[Image:2yez.jpg|left|200px]]


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==COMPLEX OF A B21 CHICKEN MHC CLASS I MOLECULE AND A 10MER CHICKEN PEPTIDE==
The line below this paragraph, containing "STRUCTURE_2yez", creates the "Structure Box" on the page.
<StructureSection load='2yez' size='340' side='right'caption='[[2yez]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[2yez]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YEZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YEZ FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#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=2yez FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yez OCA], [https://pdbe.org/2yez PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2yez RCSB], [https://www.ebi.ac.uk/pdbsum/2yez PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2yez ProSAT]</span></td></tr>
{{STRUCTURE_2yez|  PDB=2yez  |  SCENE= }}
</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.


===COMPLEX OF A B21 CHICKEN MHC CLASS I MOLECULE AND A 10MER CHICKEN PEPTIDE===
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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2yez" style="background-color:#fffaf0;"></div>


==About this Structure==
==See Also==
[[2yez]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YEZ OCA].
*[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]]
*[[MHC 3D structures|MHC 3D structures]]
*[[MHC I 3D structures|MHC I 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Chappell, P.]]
[[Category: Large Structures]]
[[Category: Harrison, M C.]]
[[Category: Chappell P]]
[[Category: Kaufman, J F.]]
[[Category: Harrison MC]]
[[Category: Lea, S M.]]
[[Category: Kaufman JF]]
[[Category: Mears, L E.]]
[[Category: Lea SM]]
[[Category: Roversi, P.]]
[[Category: Mears LE]]
[[Category: Bf21]]
[[Category: Roversi P]]
[[Category: Immune response]]
[[Category: Immune system]]
[[Category: Immunoglobulin domain]]
[[Category: Mhc i]]

Latest revision as of 11:13, 23 August 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

2yez is a 3 chain structure with sequence from Gallus gallus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.9Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

  1. 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

2yez, resolution 2.90Å

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