2rdh: Difference between revisions

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[[Image:2rdh.jpg|left|200px]]
{{Seed}}
[[Image:2rdh.png|left|200px]]


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{{STRUCTURE_2rdh|  PDB=2rdh  |  SCENE=  }}  
{{STRUCTURE_2rdh|  PDB=2rdh  |  SCENE=  }}  


'''Crystal structure of Staphylococcal Superantigen-Like protein 11'''
===Crystal structure of Staphylococcal Superantigen-Like protein 11===




==Overview==
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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.
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{{ABSTRACT_PUBMED_18045383}}


==About this Structure==
==About this Structure==
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[[Category: Ob fold]]
[[Category: Ob fold]]
[[Category: Toxin]]
[[Category: Toxin]]
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