1uns
|
IDENTIFICATION OF A SECONDARY ZINC-BINDING SITE IN STAPHYLOCOCCAL ENTEROTOXIN C2: IMPLICATIONS FOR SUPERANTIGEN RECOGNITION
OverviewOverview
The previously determined crystal structure of the superantigen, staphylococcal enterotoxin C2 (SEC2) showed binding of a single zinc ion, located between the N- and C-terminal domains. Here we present the crystal, structure of SEC2 determined to 2.0 A resolution in the presence of, additional zinc. The structure revealed the presence of a secondary, zinc-binding site close to the major histocompatibility complex, (MHC)-binding site of the toxin and some 28 A away from the primary, zinc-binding site of the toxin found in previous studies. T cell, stimulation assays showed that varying the concentration of zinc ions, present affected the activity of the toxin and we observed that high zinc, concentrations considerably inhibited T cell responses. This indicates, that SEC2 may have multiple ... [(full description)]
About this StructureAbout this Structure
1UNS is a [Single protein] structure of sequence from [Staphylococcus aureus] with ZN as [ligand]. Full crystallographic information is available from [OCA].
ReferenceReference
Identification of a secondary zinc-binding site in staphylococcal enterotoxin C2. Implications for superantigen recognition., Papageorgiou AC, Baker MD, McLeod JD, Goda SK, Manzotti CN, Sansom DM, Tranter HS, Acharya KR, J Biol Chem. 2004 Jan 9;279(2):1297-303. Epub 2003 Oct 14. PMID:14559915
Page seeded by OCA on Mon Oct 29 20:11:25 2007