1an8: Difference between revisions
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==CRYSTAL STRUCTURE OF THE STREPTOCOCCAL SUPERANTIGEN SPE-C== | ==CRYSTAL STRUCTURE OF THE STREPTOCOCCAL SUPERANTIGEN SPE-C== | ||
<StructureSection load='1an8' size='340' side='right' caption='[[1an8]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='1an8' size='340' side='right' caption='[[1an8]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1an8]] is a 1 chain structure | <table><tr><td colspan='2'>[[1an8]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AN8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AN8 FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1an8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1an8 OCA], [http://pdbe.org/1an8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1an8 RCSB], [http://www.ebi.ac.uk/pdbsum/1an8 PDBsum]</span></td></tr> | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1an8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1an8 OCA], [http://pdbe.org/1an8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1an8 RCSB], [http://www.ebi.ac.uk/pdbsum/1an8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1an8 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
</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/ | </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=1an8 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Baker, E N]] | [[Category: Baker, E N]] | ||
[[Category: Roussel, A]] | [[Category: Roussel, A]] | ||
[[Category: Bacterial superantigen]] | [[Category: Bacterial superantigen]] | ||
[[Category: Toxin]] | [[Category: Toxin]] | ||
Revision as of 12:21, 9 August 2017
CRYSTAL STRUCTURE OF THE STREPTOCOCCAL SUPERANTIGEN SPE-CCRYSTAL STRUCTURE OF THE STREPTOCOCCAL SUPERANTIGEN SPE-C
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedBacterial superantigens are small proteins that have a very potent stimulatory effect on T lymphocytes through their ability to bind to both MHC class II molecules and T-cell receptors. We have determined the three-dimensional structure of a Streptococcal superantigen, SPE-C, at 2.4 A resolution. The structure shows that SPE-C has the usual superantigen fold, but that the surface that forms a generic, low-affinity MHC-binding site in other superantigens is here used to create a SPE-C dimer. Instead, MHC class II binding occurs through a zinc binding site that is analogous to a similar site in staphylococcal enterotoxin A. Consideration of the SPE-C dimer suggests a novel mechanism for promotion of MHC aggregation and T-cell activation. Crystal structure of the streptococcal superantigen SPE-C: dimerization and zinc binding suggest a novel mode of interaction with MHC class II molecules.,Roussel A, Anderson BF, Baker HM, Fraser JD, Baker EN Nat Struct Biol. 1997 Aug;4(8):635-43. PMID:9253413[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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