8kb0: Difference between revisions
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==Crystal structure of 01JD-AEAIIVAMV== | |||
<StructureSection load='8kb0' size='340' side='right'caption='[[8kb0]], [[Resolution|resolution]] 2.48Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8kb0]] is a 6 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=8KB0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8KB0 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]] 2.48Å</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=8kb0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8kb0 OCA], [https://pdbe.org/8kb0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8kb0 RCSB], [https://www.ebi.ac.uk/pdbsum/8kb0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8kb0 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 8kb0" 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]] | |||
Latest revision as of 18:03, 29 May 2024
Crystal structure of 01JD-AEAIIVAMV
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