1an8: Difference between revisions

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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]. 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 13:48, 5 November 2007

File:1an8.gif


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. 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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