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< | ==Crystal Structure of Staphylococcal Enterotoxin G (SEG) in Complex with a Mouse T-cell Receptor beta Chain== | ||
<StructureSection load='3mc0' size='340' side='right'caption='[[3mc0]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
or | <table><tr><td colspan='2'>[[3mc0]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MC0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MC0 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]] 2Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</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=3mc0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mc0 OCA], [https://pdbe.org/3mc0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mc0 RCSB], [https://www.ebi.ac.uk/pdbsum/3mc0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mc0 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A2NTY6_MOUSE A2NTY6_MOUSE] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Superantigens (SAgs) are bacterial or viral toxins that bind MHC class II (MHC-II) molecules and T-cell receptor (TCR) in a nonconventional manner, inducing T-cell activation that leads to inflammatory cytokine production, which may result in acute toxic shock. In addition, the emerging threat of purpura fulminans and community-associated meticillin-resistant Staphylococcus aureus emphasizes the importance of a better characterization of SAg binding to their natural ligands that may allow the development of reagents to neutralize their action. The three-dimensional structure of the complex between a mouse TCR beta chain (mVbeta8.2) and staphylococcal enterotoxin G (SEG) at 2.0 A resolution revealed a binding site that does not conserve the "hot spots" present in mVbeta8.2-SEC2, mVbeta8.2-SEC3, mVbeta8.2-SEB, and mVbeta8.2-SPEA complexes. Analysis of the mVbeta8.2-SEG interface allowed us to explain the higher affinity of this complex compared with the others, which may account for the early activation of T-cells bearing mVbeta8.2 by SEG. This mode of interaction between SEG and mVbeta8.2 could be an adaptive advantage to bestow on the pathogen a faster rate of colonization of the host. | |||
Crystal structure of staphylococcal enterotoxin G (SEG) in complex with a mouse T-cell receptor {beta} chain.,Fernandez MM, Cho S, De Marzi MC, Kerzic MC, Robinson H, Mariuzza RA, Malchiodi EL J Biol Chem. 2011 Jan 14;286(2):1189-95. Epub 2010 Nov 8. PMID:21059660<ref>PMID:21059660</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3mc0" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[T-cell receptor 3D structures|T-cell receptor 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | [[Category: Large Structures]] | ||
[[ | |||
== | |||
< | |||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Staphylococcus aureus]] | [[Category: Staphylococcus aureus]] | ||
[[Category: Cho | [[Category: Cho S]] | ||
[[Category: Fernandez | [[Category: Fernandez MM]] | ||
[[Category: Malchiodi | [[Category: Malchiodi EL]] | ||
[[Category: Mariuzza | [[Category: Mariuzza RA]] | ||
[[Category: Robinson | [[Category: Robinson H]] | ||
Latest revision as of 11:51, 6 September 2023
Crystal Structure of Staphylococcal Enterotoxin G (SEG) in Complex with a Mouse T-cell Receptor beta ChainCrystal Structure of Staphylococcal Enterotoxin G (SEG) in Complex with a Mouse T-cell Receptor beta Chain
Structural highlights
FunctionPublication Abstract from PubMedSuperantigens (SAgs) are bacterial or viral toxins that bind MHC class II (MHC-II) molecules and T-cell receptor (TCR) in a nonconventional manner, inducing T-cell activation that leads to inflammatory cytokine production, which may result in acute toxic shock. In addition, the emerging threat of purpura fulminans and community-associated meticillin-resistant Staphylococcus aureus emphasizes the importance of a better characterization of SAg binding to their natural ligands that may allow the development of reagents to neutralize their action. The three-dimensional structure of the complex between a mouse TCR beta chain (mVbeta8.2) and staphylococcal enterotoxin G (SEG) at 2.0 A resolution revealed a binding site that does not conserve the "hot spots" present in mVbeta8.2-SEC2, mVbeta8.2-SEC3, mVbeta8.2-SEB, and mVbeta8.2-SPEA complexes. Analysis of the mVbeta8.2-SEG interface allowed us to explain the higher affinity of this complex compared with the others, which may account for the early activation of T-cells bearing mVbeta8.2 by SEG. This mode of interaction between SEG and mVbeta8.2 could be an adaptive advantage to bestow on the pathogen a faster rate of colonization of the host. Crystal structure of staphylococcal enterotoxin G (SEG) in complex with a mouse T-cell receptor {beta} chain.,Fernandez MM, Cho S, De Marzi MC, Kerzic MC, Robinson H, Mariuzza RA, Malchiodi EL J Biol Chem. 2011 Jan 14;286(2):1189-95. Epub 2010 Nov 8. PMID:21059660[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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