6ilc: Difference between revisions
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<StructureSection load='6ilc' size='340' side='right'caption='[[6ilc]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='6ilc' size='340' side='right'caption='[[6ilc]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6ilc]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ILC OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[6ilc]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Henipavirus_hendraense Henipavirus hendraense] and [https://en.wikipedia.org/wiki/Pteropus_alecto Pteropus alecto]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ILC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ILC FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</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=6ilc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ilc OCA], [https://pdbe.org/6ilc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ilc RCSB], [https://www.ebi.ac.uk/pdbsum/6ilc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ilc ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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</div> | </div> | ||
<div class="pdbe-citations 6ilc" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 6ilc" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[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 == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Henipavirus hendraense]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Pteropus alecto]] | ||
[[Category: | [[Category: Qu ZH]] | ||
[[Category: | [[Category: Xia C]] | ||
[[Category: | [[Category: Zhang NZ]] | ||
Latest revision as of 11:03, 17 October 2024
CRYSTAL STRUCTURE OF BAT MHC CLASS I PTAL-N*01:01 FOR 2.2 ANGSTROMCRYSTAL STRUCTURE OF BAT MHC CLASS I PTAL-N*01:01 FOR 2.2 ANGSTROM
Structural highlights
Publication Abstract from PubMedBats are natural reservoir hosts, harboring more than 100 viruses, some of which are lethal to humans. The asymptomatic coexistence with viruses is thought to be connected to the unique immune system of bats. MHC class I (MHC I) presentation is closely related to cytotoxic lymphocyte immunity, which plays an important role in viral resistance. To investigate the characteristics of MHC I presentation in bats, the crystal structures of peptide-MHC I complexes of Pteropus alecto, Ptal-N*01:01/HEV-1 (DFANTFLP) and Ptal-N*01:01/HEV-2 (DYINTNLVP), and two related mutants, Ptal-N*01:01/HEV-1POmegaL (DFANTFLL) and Ptal-N*01:01DeltaMDL/HEV-1, were determined. Through structural analysis, we found that Ptal-N*01:01 had a multi-Ala-assembled pocket B and a flexible hydrophobic pocket F, which could accommodate variable anchor residues and allow Ptal-N*01:01 to bind numerous peptides. Three sequential amino acids, Met, Asp, and Leu, absent from the alpha1 domain of the H chain in other mammals, were present in this domain in the bat. Upon deleting these amino acids and determining the structure in p/Ptal-N*01:01DeltaMDL/HEV-1, we found they helped form an extra salt-bridge chain between the H chain and the N-terminal aspartic acid of the peptide. By introducing an MHC I random peptide library for de novo liquid chromatography-tandem mass spectrometry analysis, we found that this insertion module, present in all types of bats, can promote MHC I presentation of peptides with high affinity during the peptide exchange process. This study will help us better understand how bat MHC I presents high-affinity peptides from an extensive binding peptidome and provides a foundation to understand the cellular immunity of bats. Structure and Peptidome of the Bat MHC Class I Molecule Reveal a Novel Mechanism Leading to High-Affinity Peptide Binding.,Qu Z, Li Z, Ma L, Wei X, Zhang L, Liang R, Meng G, Zhang N, Xia C J Immunol. 2019 Jun 15;202(12):3493-3506. doi: 10.4049/jimmunol.1900001. Epub, 2019 May 10. PMID:31076531[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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