1l0y
From Proteopedia
(Difference between revisions)
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<StructureSection load='1l0y' size='340' side='right'caption='[[1l0y]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='1l0y' size='340' side='right'caption='[[1l0y]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1l0y]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1l0y]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Streptococcus_pyogenes Streptococcus pyogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L0Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1L0Y FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> |
| - | <tr id=' | + | <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=ZN:ZINC+ION'>ZN</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=1l0y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l0y OCA], [https://pdbe.org/1l0y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l0y RCSB], [https://www.ebi.ac.uk/pdbsum/1l0y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l0y ProSAT]</span></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=1l0y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l0y OCA], [https://pdbe.org/1l0y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l0y RCSB], [https://www.ebi.ac.uk/pdbsum/1l0y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l0y ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/TCB2_MOUSE TCB2_MOUSE] | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1l0y ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1l0y ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Superantigens (SAGs) crosslink MHC class II and TCR molecules, resulting in an overstimulation of T cells associated with human disease. SAGs interact with several different surfaces on MHC molecules, necessitating the formation of multiple distinct MHC-SAG-TCR ternary signaling complexes. Variability in SAG-TCR binding modes could also contribute to the structural heterogeneity of SAG-dependent signaling complexes. We report crystal structures of the streptococcal SAGs SpeA and SpeC in complex with their corresponding TCR beta chain ligands that reveal distinct TCR binding modes. The SpeC-TCR beta chain complex structure, coupled with the recently determined SpeC-HLA-DR2a complex structure, provides a model for a novel T cell signaling complex that precludes direct TCR-MHC interactions. Thus, highly efficient T cell activation may be achieved through structurally diverse strategies of TCR ligation. | ||
| - | |||
| - | Structures of two streptococcal superantigens bound to TCR beta chains reveal diversity in the architecture of T cell signaling complexes.,Sundberg EJ, Li H, Llera AS, McCormick JK, Tormo J, Schlievert PM, Karjalainen K, Mariuzza RA Structure. 2002 May;10(5):687-99. PMID:12015151<ref>PMID:12015151</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1l0y" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Exotoxin 3D structures|Exotoxin 3D structures]] | *[[Exotoxin 3D structures|Exotoxin 3D structures]] | ||
*[[T-cell receptor 3D structures|T-cell receptor 3D structures]] | *[[T-cell receptor 3D structures|T-cell receptor 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Micrococcus scarlatinae klein 1884]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Mus musculus]] |
| - | [[Category: | + | [[Category: Streptococcus pyogenes]] |
| - | [[Category: | + | [[Category: Li H]] |
| - | [[Category: | + | [[Category: Mariuzza RA]] |
| - | [[Category: | + | [[Category: Sundberg EJ]] |
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Revision as of 08:05, 3 April 2024
T cell receptor beta chain complexed with superantigen SpeA soaked with zinc
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