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7qhp
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of I-Ag7 with a bound hybrid insulin peptide== | |
| + | <StructureSection load='7qhp' size='340' side='right'caption='[[7qhp]], [[Resolution|resolution]] 1.82Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7qhp]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7QHP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QHP 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]] 1.82Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=7qhp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qhp OCA], [https://pdbe.org/7qhp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qhp RCSB], [https://www.ebi.ac.uk/pdbsum/7qhp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qhp ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/HA2D_MOUSE HA2D_MOUSE] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | We recently provided evidence for promiscuous recognition of several different hybrid insulin peptides (HIPs) by the highly diabetogenic, I-A(g7)-restricted 4.1-T cell receptor (TCR). To understand the structural determinants of this phenomenon, we solved the structure of an agonistic HIP/I-A(g7) complex, both in isolation as well as bound to the 4.1-TCR. We find that HIP promiscuity of the 4.1-TCR is dictated, on the one hand, by an amino acid sequence pattern that ensures I-A(g7) binding and, on the other hand, by the presence of three acidic residues at positions P5, P7 and P8 that favor an optimal engagement by the 4.1-TCR's complementary determining regions. Surprisingly, comparison of the TCR-bound and unbound HIP/I-A(g7) structures reveals that 4.1-TCR binding triggers several novel and unique structural motions in both the I-A(g7) molecule and the peptide that are essential for docking. This observation indicates that the type 1 diabetes-associated I-A(g7) molecule is structurally malleable and that this plasticity allows the recognition of multiple peptides by individual TCRs that would otherwise be unable to do so. | ||
| - | + | Structural plasticity in I-A(g7) links autoreactivity to hybrid insulin peptides in type I diabetes.,Erausquin E, Serra P, Parras D, Santamaria P, Lopez-Sagaseta J Front Immunol. 2022 Jul 28;13:924311. doi: 10.3389/fimmu.2022.924311. eCollection, 2022. PMID:35967292<ref>PMID:35967292</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 7qhp" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[MHC 3D structures|MHC 3D structures]] | ||
| + | *[[MHC II 3D structures|MHC II 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Mus musculus]] | ||
| + | [[Category: Erausquin E]] | ||
| + | [[Category: Lopez-Sagaseta J]] | ||
Current revision
Structure of I-Ag7 with a bound hybrid insulin peptide
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