6lbe: Difference between revisions
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The | ==Crystal structure of bony fish MHC class I binding beta2M-2 for 2.6 angstrom== | ||
<StructureSection load='6lbe' size='340' side='right'caption='[[6lbe]], [[Resolution|resolution]] 2.60Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6lbe]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Ctenopharyngodon_idella Ctenopharyngodon idella] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LBE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6LBE 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]] 2.6Å</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=6lbe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lbe OCA], [https://pdbe.org/6lbe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6lbe RCSB], [https://www.ebi.ac.uk/pdbsum/6lbe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6lbe ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q65XY8_CTEID Q65XY8_CTEID] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Contemporary antigen presentation knowledge is based on the existence of a single beta2m locus, and a classical MHC class I forms a complex with a peptide (i.e., pMHC-I) to trigger CTL immunity. However, two beta2m loci have been found in diploid bony fish; the function of the two beta2m molecules is unclear. Here, we determined the variant peptide profiles originating from different products of the beta2m loci binding to the same MHC-I molecule and further solved the crystal structures of the two pMHC-I molecules (i.e., pCtid-UAA-beta2m-2 and pCtid-UAA-beta2m-1-II). Of note, in pCtid-UAA-beta2m-2, a unique hydrogen bond network formed in the bottom of the peptide-binding groove (PBG) led to alpha2-helix drift, ultimately leading to structural changes in the PBG. The mechanism of the change in peptide presentation profiles by beta2m molecules is illustrated. The results are also of great significance for antivirus and antitumor functions in cold-blooded vertebrates and even humans. | |||
The Mechanism of beta2m Molecule-Induced Changes in the Peptide Presentation Profile in a Bony Fish.,Li Z, Zhang N, Ma L, Zhang L, Meng G, Xia C iScience. 2020 May 22;23(5):101119. doi: 10.1016/j.isci.2020.101119. Epub 2020, Apr 30. PMID:32438322<ref>PMID:32438322</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 6lbe" style="background-color:#fffaf0;"></div> | ||
[[Category: Li | |||
==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/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Ctenopharyngodon idella]] | |||
[[Category: Large Structures]] | |||
[[Category: Synthetic construct]] | |||
[[Category: Li ZB]] | |||
[[Category: Xia C]] | |||
Latest revision as of 13:55, 22 November 2023
Crystal structure of bony fish MHC class I binding beta2M-2 for 2.6 angstromCrystal structure of bony fish MHC class I binding beta2M-2 for 2.6 angstrom
Structural highlights
FunctionPublication Abstract from PubMedContemporary antigen presentation knowledge is based on the existence of a single beta2m locus, and a classical MHC class I forms a complex with a peptide (i.e., pMHC-I) to trigger CTL immunity. However, two beta2m loci have been found in diploid bony fish; the function of the two beta2m molecules is unclear. Here, we determined the variant peptide profiles originating from different products of the beta2m loci binding to the same MHC-I molecule and further solved the crystal structures of the two pMHC-I molecules (i.e., pCtid-UAA-beta2m-2 and pCtid-UAA-beta2m-1-II). Of note, in pCtid-UAA-beta2m-2, a unique hydrogen bond network formed in the bottom of the peptide-binding groove (PBG) led to alpha2-helix drift, ultimately leading to structural changes in the PBG. The mechanism of the change in peptide presentation profiles by beta2m molecules is illustrated. The results are also of great significance for antivirus and antitumor functions in cold-blooded vertebrates and even humans. The Mechanism of beta2m Molecule-Induced Changes in the Peptide Presentation Profile in a Bony Fish.,Li Z, Zhang N, Ma L, Zhang L, Meng G, Xia C iScience. 2020 May 22;23(5):101119. doi: 10.1016/j.isci.2020.101119. Epub 2020, Apr 30. PMID:32438322[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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