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2rdh

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[[Image:2rdh.jpg|left|200px]]
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{{Structure
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|GENE= SSL11 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 Staphylococcus aureus])
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{{STRUCTURE_2rdh| PDB=2rdh | SCENE= }}
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|RELATEDENTRY=[[2rdg|2RDG]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2rdh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rdh OCA], [http://www.ebi.ac.uk/pdbsum/2rdh PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2rdh RCSB]</span>
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'''Crystal structure of Staphylococcal Superantigen-Like protein 11'''
'''Crystal structure of Staphylococcal Superantigen-Like protein 11'''
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[[Category: Langley, R J.]]
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Revision as of 13:41, 4 May 2008

Template:STRUCTURE 2rdh

Crystal structure of Staphylococcal Superantigen-Like protein 11


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

2RDH 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 16:41:33 2008

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