1an8

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[[Image:1an8.jpg|left|200px]]
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{{STRUCTURE_1an8| PDB=1an8 | SCENE= }}
{{STRUCTURE_1an8| PDB=1an8 | SCENE= }}
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'''CRYSTAL STRUCTURE OF THE STREPTOCOCCAL SUPERANTIGEN SPE-C'''
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===CRYSTAL STRUCTURE OF THE STREPTOCOCCAL SUPERANTIGEN SPE-C===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 9253413 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9253413}}
==About this Structure==
==About this Structure==
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[[Category: Bacterial superantigen]]
[[Category: Bacterial superantigen]]
[[Category: Toxin]]
[[Category: Toxin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 17:12:26 2008''

Revision as of 14:12, 30 June 2008

Template:STRUCTURE 1an8

CRYSTAL STRUCTURE OF THE STREPTOCOCCAL SUPERANTIGEN SPE-C

Template:ABSTRACT PUBMED 9253413

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

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