1an8: Difference between revisions
New page: left|200px<br /> <applet load="1an8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1an8, resolution 2.4Å" /> '''CRYSTAL STRUCTURE OF... |
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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]]. 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]]. Structure known Active Sites: ZNA and ZNB. 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 11:52, 30 October 2007
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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]. Structure known Active Sites: ZNA and ZNB. 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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