1an8: Difference between revisions

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[[Image:1an8.gif|left|200px]]<br />
[[Image:1an8.jpg|left|200px]]<br /><applet load="1an8" size="450" color="white" frame="true" align="right" spinBox="true"  
<applet load="1an8" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1an8, resolution 2.4&Aring;" />
caption="1an8, resolution 2.4&Aring;" />
'''CRYSTAL STRUCTURE OF THE STREPTOCOCCAL SUPERANTIGEN SPE-C'''<br />
'''CRYSTAL STRUCTURE OF THE STREPTOCOCCAL SUPERANTIGEN SPE-C'''<br />
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==About this Structure==
==About this Structure==
1AN8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_pyogenes Streptococcus pyogenes]. Structure known Active Sites: ZNA and ZNB. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AN8 OCA].  
1AN8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_pyogenes Streptococcus pyogenes]. Known structural/functional Sites: <scene name='pdbsite=ZNA:This Site Also Includes HIS 81 From A Symmetry-Related M ...'>ZNA</scene> and <scene name='pdbsite=ZNB:This Site Also Includes HIS 35 And GLU 54 From A Symmetr ...'>ZNB</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AN8 OCA].  


==Reference==
==Reference==
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[[Category: toxin]]
[[Category: toxin]]


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Revision as of 15:08, 18 December 2007

File:1an8.jpg


1an8, resolution 2.4Å

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CRYSTAL STRUCTURE OF THE STREPTOCOCCAL SUPERANTIGEN SPE-C

OverviewOverview

Bacterial 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.

About this StructureAbout this Structure

1AN8 is a Single protein structure of sequence from Streptococcus pyogenes. Known structural/functional Sites: and . Full crystallographic information is available from OCA.

ReferenceReference

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

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