7tud: Difference between revisions
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New page: '''Unreleased structure''' The entry 7tud is ON HOLD Authors: Jiang, J., Natarajan, K., Kim, E., Boyd, L.F., Margulies, D.H. Description: Crystal structure of HLA-B*44:05 (T73C) with 6... |
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The | ==Crystal structure of HLA-B*44:05 (T73C) with 6mer EEFGRC and dipeptide GL== | ||
<StructureSection load='7tud' size='340' side='right'caption='[[7tud]], [[Resolution|resolution]] 1.45Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7tud]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] 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=7TUD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7TUD 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]] 1.45Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <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'>[https://proteopedia.org/fgij/fg.htm?mol=7tud FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7tud OCA], [https://pdbe.org/7tud PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7tud RCSB], [https://www.ebi.ac.uk/pdbsum/7tud PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7tud ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/D5H3J5_HUMAN D5H3J5_HUMAN] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Loading of MHC-I molecules with peptide by the catalytic chaperone tapasin in the peptide loading complex plays a critical role in antigen presentation and immune recognition. Mechanistic insight has been hampered by the lack of detailed structural information concerning tapasin-MHC-I. We present here crystal structures of human tapasin complexed with the MHC-I molecule HLA-B*44:05, and with each of two anti-tapasin antibodies. The tapasin-stabilized peptide-receptive state of HLA-B*44:05 is characterized by distortion of the peptide binding groove and destabilization of the beta(2)-microglobulin interaction, leading to release of peptide. Movements of the membrane proximal Ig-like domains of tapasin, HLA-B*44:05, and beta(2)-microglobulin accompany the transition to a peptide-receptive state. Together this ensemble of crystal structures provides insights into a distinct mechanism of tapasin-mediated peptide exchange. | |||
Structural mechanism of tapasin-mediated MHC-I peptide loading in antigen presentation.,Jiang J, Taylor DK, Kim EJ, Boyd LF, Ahmad J, Mage MG, Truong HV, Woodward CH, Sgourakis NG, Cresswell P, Margulies DH, Natarajan K Nat Commun. 2022 Sep 17;13(1):5470. doi: 10.1038/s41467-022-33153-8. PMID:36115831<ref>PMID:36115831</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 7tud" style="background-color:#fffaf0;"></div> | ||
[[Category: Boyd | |||
[[Category: | ==See Also== | ||
[[Category: Margulies | *[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]] | ||
[[Category: | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Synthetic construct]] | |||
[[Category: Boyd LF]] | |||
[[Category: Jiang J]] | |||
[[Category: Kim E]] | |||
[[Category: Margulies DH]] | |||
[[Category: Natarajan K]] | |||