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8kb1
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of 11JD== | |
| + | <StructureSection load='8kb1' size='340' side='right'caption='[[8kb1]], [[Resolution|resolution]] 2.46Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8kb1]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Anas_platyrhynchos Anas platyrhynchos] and [https://en.wikipedia.org/wiki/Unidentified_influenza_virus Unidentified influenza virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8KB1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8KB1 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]] 2.46Å</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=8kb1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8kb1 OCA], [https://pdbe.org/8kb1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8kb1 RCSB], [https://www.ebi.ac.uk/pdbsum/8kb1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8kb1 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q14U75_ANAPL Q14U75_ANAPL] Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system.[SAAS:SAAS00319106] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Micropolymorphism significantly shapes the peptide-binding characteristics of major histocompatibility complex class I (MHC-I) molecules, affecting the host's resistance to pathogens, which is particularly pronounced in avian species displaying the "minimal essential MHC" expression pattern. In this study, we compared two duck MHC-I alleles, Anpl-UAA*77 and Anpl-UAA*78, that exhibit markedly different peptide binding properties despite their high sequence homology. Through mutagenesis experiments and crystallographic analysis of complexes with the influenza virus-derived peptide AEAIIVAMV (AEV9), we identified a critical role for the residue at position 62 in regulating hydrogen-bonding interactions between the peptide backbone and the peptide-binding groove. This modulation affects the characteristics of the B pocket and the stability of the loop region between the 3(10) helix and the alpha1 helix, leading to significant changes in the structure and stability of the peptide-MHC-I complex (pMHC-I). Moreover, the proportion of different residues at position 62 among Anpl-UAAs may reflect the correlation between pAnpl-UAA stability and duck body temperature. This research not only advances our understanding of the Anpl-UAA structure but also deepens our insight into the impact of MHC-I micropolymorphism on peptide binding. | ||
| - | + | The impact of micropolymorphism in Anpl-UAA on structural stability and peptide presentation.,Tang Z, Wang S, Du L, Hu D, Chen X, Zheng H, Ding H, Chen S, Zhang L, Zhang N Int J Biol Macromol. 2024 May;267(Pt 2):131665. doi: , 10.1016/j.ijbiomac.2024.131665. Epub 2024 Apr 16. PMID:38636758<ref>PMID:38636758</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 8kb1" style="background-color:#fffaf0;"></div> |
| - | [[Category: Tang | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Anas platyrhynchos]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Unidentified influenza virus]] | ||
| + | [[Category: Tang Z]] | ||
| + | [[Category: Zhang N]] | ||
Current revision
Crystal structure of 11JD
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