6wl3: Difference between revisions
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==== | ==preTCRbeta-pMHC complex crystal structure== | ||
<StructureSection load='6wl3' size='340' side='right'caption='[[6wl3]]' scene=''> | <StructureSection load='6wl3' size='340' side='right'caption='[[6wl3]], [[Resolution|resolution]] 3.45Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[6wl3]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Vesicular_stomatitis_virus Vesicular stomatitis virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6WL3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6WL3 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]] 3.45Å</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=6wl3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6wl3 OCA], [https://pdbe.org/6wl3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6wl3 RCSB], [https://www.ebi.ac.uk/pdbsum/6wl3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6wl3 ProSAT]</span></td></tr> | |||
</table> | </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> | |||
</div> | |||
<div class="pdbe-citations 6wl3" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[MHC 3D structures|MHC 3D structures]] | |||
*[[MHC I 3D structures|MHC I 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Mus musculus]] | ||
[[Category: Vesicular stomatitis virus]] | |||
[[Category: Li X]] | |||
[[Category: Mallis RJ]] | |||
[[Category: Mizsei R]] | |||
[[Category: Reinherz EL]] | |||
[[Category: Tan K]] | |||
[[Category: Wang J]] | |||
Latest revision as of 17:30, 18 October 2023
preTCRbeta-pMHC complex crystal structurepreTCRbeta-pMHC complex crystal structure
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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