This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1an8
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /> <applet load="1an8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1an8, resolution 2.4Å" /> '''CRYSTAL STRUCTURE OF...)
Next diff →
Revision as of 14:57, 29 October 2007
|
CRYSTAL STRUCTURE OF THE STREPTOCOCCAL SUPERANTIGEN SPE-C
Overview
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 Structure
1AN8 is a [Single protein] structure of sequence from [Streptococcus pyogenes]. Full crystallographic information is available from [OCA].
Reference
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
Page seeded by OCA on Mon Oct 29 17:01:52 2007
