7ji2: Difference between revisions
New page: '''Unreleased structure''' The entry 7ji2 is ON HOLD Authors: Li, X., Mallis, R.J., Mizsei, R., Tan, K., Reinherz, E.L., Wang, J. Description: preTCRbeta-pMHC complex crystal structure... |
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==Crystal Structure of H2-Kb in complex with a OVA mutant peptide== | |||
<StructureSection load='7ji2' size='340' side='right'caption='[[7ji2]], [[Resolution|resolution]] 1.95Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7ji2]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus_bactrianus Mus musculus bactrianus] 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=7JI2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7JI2 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]] 1.95Å</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></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=7ji2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ji2 OCA], [https://pdbe.org/7ji2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ji2 RCSB], [https://www.ebi.ac.uk/pdbsum/7ji2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ji2 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/HA1B_MOUSE HA1B_MOUSE] Involved in the presentation of foreign antigens to the immune system. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Self-discrimination, a critical but ill-defined molecular process programmed during thymocyte development, requires myriad pre-T cell receptors (preTCRs) and alphabetaTCRs. Using x-ray crystallography, we show how a preTCR applies the concave beta-sheet surface of its single variable domain (Vbeta) to "horizontally" grab the protruding MHC alpha2-helix. By contrast, alphabetaTCRs purpose all six complementarity-determining region (CDR) loops of their paired ValphaVbeta module to recognize peptides bound to major histocompatibility complex molecules (pMHCs) in "vertical" head-to-head binding. The preTCR topological fit ensures that CDR3beta reaches the peptide's featured C-terminal segment for pMHC sampling, establishing the subsequent alphabetaTCR canonical docking mode. "Horizontal" docking precludes germline CDR1beta- and CDR2beta-MHC binding to broaden beta-chain repertoire diversification before alphabetaTCR-mediated selection refinement. Thus, one subunit successively attunes the recognition logic of related multicomponent receptors. | |||
Pre-T cell receptors topologically sample self-ligands during thymocyte beta-selection.,Li X, Mizsei R, Tan K, Mallis RJ, Duke-Cohan JS, Akitsu A, Tetteh PW, Dubey A, Hwang W, Wagner G, Lang MJ, Arthanari H, Wang JH, Reinherz EL Science. 2021 Jan 8;371(6525):181-185. doi: 10.1126/science.abe0918. Epub 2020 , Dec 17. PMID:33335016<ref>PMID:33335016</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 7ji2" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: | ==See Also== | ||
[[Category: Mallis | *[[Beta-2 microglobulin 3D structures|Beta-2 microglobulin 3D structures]] | ||
[[Category: | *[[MHC 3D structures|MHC 3D structures]] | ||
[[Category: | *[[MHC I 3D structures|MHC I 3D structures]] | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mus musculus bactrianus]] | |||
[[Category: Synthetic construct]] | |||
[[Category: Li X]] | |||
[[Category: Mallis RJ]] | |||
[[Category: Mizsei R]] | |||
[[Category: Reinherz EL]] | |||
[[Category: Tan K]] | |||
[[Category: Wang J]] | |||
Latest revision as of 18:03, 18 October 2023
Crystal Structure of H2-Kb in complex with a OVA mutant peptideCrystal Structure of H2-Kb in complex with a OVA mutant peptide
Structural highlights
FunctionHA1B_MOUSE Involved in the presentation of foreign antigens to the immune system. Publication Abstract from PubMedSelf-discrimination, a critical but ill-defined molecular process programmed during thymocyte development, requires myriad pre-T cell receptors (preTCRs) and alphabetaTCRs. Using x-ray crystallography, we show how a preTCR applies the concave beta-sheet surface of its single variable domain (Vbeta) to "horizontally" grab the protruding MHC alpha2-helix. By contrast, alphabetaTCRs purpose all six complementarity-determining region (CDR) loops of their paired ValphaVbeta module to recognize peptides bound to major histocompatibility complex molecules (pMHCs) in "vertical" head-to-head binding. The preTCR topological fit ensures that CDR3beta reaches the peptide's featured C-terminal segment for pMHC sampling, establishing the subsequent alphabetaTCR canonical docking mode. "Horizontal" docking precludes germline CDR1beta- and CDR2beta-MHC binding to broaden beta-chain repertoire diversification before alphabetaTCR-mediated selection refinement. Thus, one subunit successively attunes the recognition logic of related multicomponent receptors. Pre-T cell receptors topologically sample self-ligands during thymocyte beta-selection.,Li X, Mizsei R, Tan K, Mallis RJ, Duke-Cohan JS, Akitsu A, Tetteh PW, Dubey A, Hwang W, Wagner G, Lang MJ, Arthanari H, Wang JH, Reinherz EL Science. 2021 Jan 8;371(6525):181-185. doi: 10.1126/science.abe0918. Epub 2020 , Dec 17. PMID:33335016[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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