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'''Crystal structure of Staphylococcal Superantigen-Like protein 11 in complex with Sialyl Lewis X''' | '''Crystal structure of Staphylococcal Superantigen-Like protein 11 in complex with Sialyl Lewis X''' | ||
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[[Category: Langley, R J.]] | [[Category: Langley, R J.]] | ||
[[Category: Wines, B D.]] | [[Category: Wines, B D.]] | ||
[[Category: | [[Category: Beta grasp]] | ||
[[Category: | [[Category: Ob fold]] | ||
[[Category: | [[Category: Protein-carbohydrate complex]] | ||
[[Category: | [[Category: Toxin]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 16:41:17 2008'' | |||
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Revision as of 13:41, 4 May 2008
Crystal structure of Staphylococcal Superantigen-Like protein 11 in complex with Sialyl Lewis X
Overview
Staphylococcus aureus is a major pathogen that produces a family of 14 staphylococcal superantigen-like (SSL) proteins, which are structurally similar to superantigens but do not stimulate T cells. SSL11 is one member of the family that is found in all staphylococcal strains. Recombinant SSL11 bound to granulocytes and monocytes through a sialic acid-dependent mechanism and was rapidly internalized. SSL11 also bound to sialic acid-containing glycoproteins, such as the Fc receptor for IgA (FcalphaRI) and P-selectin glycoprotein ligand-1 (PSGL-1), and inhibited neutrophil attachment to a P-selectin-coated surface. Biosensor analysis of two SSL11 alleles binding to sialyl Lewis X [sLe(x)- Neu5Acalpha2-3Galbeta1-4(Fuc1-3)GlcNAc] coupled to bovine serum albumin gave dissociation constants of 0.7 and 7 mum respectively. Binding of SSL11 to a glycan array revealed specificity for glycans containing the trisaccharide sialyllactosamine (sLacNac - Neu5Acalpha2-3Galbeta1-4GlcNAc). A 1.6 A resolution crystal structure of SSL11 complexed with sLe(x) revealed a discrete binding site in the C-terminal beta-grasp domain, with predominant interactions with the sialic acid and galactose residues. A single amino acid mutation in the carbohydrate binding site abolished all SSL11 binding. Thus, SSL11 is a staphylococcal protein that targets myeloid cells by binding sialyllactosamine-containing glycoproteins.
About this Structure
2RDG is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.
Reference
The crystal structure of staphylococcal superantigen-like protein 11 in complex with sialyl Lewis X reveals the mechanism for cell binding and immune inhibition., Chung MC, Wines BD, Baker H, Langley RJ, Baker EN, Fraser JD, Mol Microbiol. 2007 Dec;66(6):1342-55. PMID:18045383 Page seeded by OCA on Sun May 4 16:41:17 2008
