6kvm: Difference between revisions
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<StructureSection load='6kvm' size='340' side='right'caption='[[6kvm]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='6kvm' size='340' side='right'caption='[[6kvm]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6kvm]] is a 3 chain structure with sequence from [ | <table><tr><td colspan='2'>[[6kvm]] 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=6KVM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6KVM FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.897Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6kvm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kvm OCA], [https://pdbe.org/6kvm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6kvm RCSB], [https://www.ebi.ac.uk/pdbsum/6kvm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6kvm ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q4U5Z6_CHICK Q4U5Z6_CHICK] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 6kvm" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 6kvm" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[MHC 3D structures|MHC 3D structures]] | |||
*[[MHC II 3D structures|MHC II 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Gallus gallus]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Xia | [[Category: Xia C]] | ||
[[Category: Zhang | [[Category: Zhang L]] | ||
Latest revision as of 13:44, 22 November 2023
Crystal structure of Chicken MHC Class II for 1.9 angstromCrystal structure of Chicken MHC Class II for 1.9 angstrom
Structural highlights
FunctionPublication Abstract from PubMedMHC class II (MHC-II) molecules play a crucial role in cellular and humoral immunity by forming peptide-MHC-II (pMHC-II) complexes. The three-dimensional structures of pMHC-II complexes have been well resolved in humans and mice. However, there is no structural information for pMHC-II complexes in nonmammals. In chickens, there are two closely related and highly polymorphic beta-chains and one monomorphic alpha-chain, and the mechanism by which one monomorphic alpha-chain combines with two polymorphic beta-chains to form a functional heterodimer remains unknown. In this study, we report the crystal structure of a chicken pMHC-II complex (pBL2*019:01) at 1.9-A resolution as the first nonmammalian structure of a pMHC-II complex. The structure reveals an increase in hydrogen bonding between the alpha and beta main chains at the central interface that is introduced by the insertion of four residues in the alpha-chain. The residues in the beta-chain that form hydrogen bonds with the alpha-chain are conserved among all beta alleles. These structural characteristics explain the phenomenon of only one BLA allele without sequence variation pairing with highly diverse BLB alleles from two loci in the genome. Additionally, the characteristics of the peptide in the peptide-binding groove were confirmed. These results provide a new understanding of the pairing mechanism of the alpha- and beta-chains in a pMHC-II complex and establish a structural principle to design epitope-related vaccines for the prevention of chicken diseases. A Newly Recognized Pairing Mechanism of the alpha- and beta-Chains of the Chicken Peptide-MHC Class II Complex.,Zhang L, Li X, Ma L, Zhang B, Meng G, Xia C J Immunol. 2020 Mar 15;204(6):1630-1640. doi: 10.4049/jimmunol.1901305. Epub 2020, Feb 7. PMID:32034060[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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