| Structural highlights
5i4d is a 2 chain structure with sequence from Staphylococcus aureus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 1.75Å |
| Ligands: | FUC, GAL, NAG, NDG, PG4, PGE, PRD_900122, SIA |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
SSL3_STAA8 Secreted protein that plays an essential role in immune innate response inhibition by interacting with and inhibiting host TLR2. In turn, bacteria recognition by immune cells is impaired and cytokine production is inhibited (PubMed:22665377, PubMed:22714643). Mechanistically, by interacting with TLR2, blocks ligand binding and thus inhibits activation (PubMed:26283364). Second, by interacting with an already formed TLR2-lipopeptide complex, prevents TLR heterodimerization and downstream signaling. The interaction with host TLR2 does not involve sialyl Lewis X interactions (PubMed:26283364).[1] [2] [3]
References
- ↑ Yokoyama R, Itoh S, Kamoshida G, Takii T, Fujii S, Tsuji T, Onozaki K. Staphylococcal superantigen-like protein 3 binds to the Toll-like receptor 2 extracellular domain and inhibits cytokine production induced by Staphylococcus aureus, cell wall component, or lipopeptides in murine macrophages. Infect Immun. 2012 Aug;80(8):2816-25. PMID:22665377 doi:10.1128/IAI.00399-12
- ↑ Bardoel BW, Vos R, Bouman T, Aerts PC, Bestebroer J, Huizinga EG, Brondijk TH, van Strijp JA, de Haas CJ. Evasion of Toll-like receptor 2 activation by staphylococcal superantigen-like protein 3. J Mol Med (Berl). 2012 Oct;90(10):1109-20. PMID:22714643 doi:10.1007/s00109-012-0926-8
- ↑ Koymans KJ, Feitsma LJ, Brondijk TH, Aerts PC, Lukkien E, Lossl P, van Kessel KP, de Haas CJ, van Strijp JA, Huizinga EG. Structural basis for inhibition of TLR2 by staphylococcal superantigen-like protein 3 (SSL3). Proc Natl Acad Sci U S A. 2015 Aug 17. pii: 201502026. PMID:26283364 doi:https://dx.doi.org/10.1073/pnas.1502026112
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