View source for 3owe


==Crystal Structure of Staphylococcal Enterotoxin G (SEG) in Complex with a High Affinity Mutant Mouse T-cell Receptor Chain==
<StructureSection load='3owe' size='340' side='right'caption='[[3owe]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3owe]] is a 16 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=3OWE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OWE 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]] 2.6&#8491;</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=3owe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3owe OCA], [https://pdbe.org/3owe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3owe RCSB], [https://www.ebi.ac.uk/pdbsum/3owe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3owe 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3owe" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Staphylococcus aureus]]
[[Category: Cho S]]
[[Category: Fernandez MM]]
[[Category: Malchiodi ML]]
[[Category: Mariuzza RA]]
[[Category: Robinson H]]