2z82

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Crystal structure of the TLR1-TLR2 heterodimer induced by binding of a tri-acylated lipopeptide

Structural highlights

2z82 is a 1 chain structure with sequence from Eptatretus burgeri and Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.6Å
Ligands:MAN, NAG, PDJ
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TLR2_MOUSE Cooperates with LY96 to mediate the innate immune response to bacterial lipoproteins and other microbial cell wall components. Cooperates with TLR1 or TLR6 to mediate the innate immune response to bacterial lipoproteins or lipopeptides. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. May also promote apoptosis in response to lipoproteins (By similarity).[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

TLR2 in association with TLR1 or TLR6 plays an important role in the innate immune response by recognizing microbial lipoproteins and lipopeptides. Here we present the crystal structures of the human TLR1-TLR2-lipopeptide complex and of the mouse TLR2-lipopeptide complex. Binding of the tri-acylated lipopeptide, Pam(3)CSK(4), induced the formation of an "m" shaped heterodimer of the TLR1 and TLR2 ectodomains whereas binding of the di-acylated lipopeptide, Pam(2)CSK(4), did not. The three lipid chains of Pam(3)CSK(4) mediate the heterodimerization of the receptor; the two ester-bound lipid chains are inserted into a pocket in TLR2, while the amide-bound lipid chain is inserted into a hydrophobic channel in TLR1. An extensive hydrogen-bonding network, as well as hydrophobic interactions, between TLR1 and TLR2 further stabilize the heterodimer. We propose that formation of the TLR1-TLR2 heterodimer brings the intracellular TIR domains close to each other to promote dimerization and initiate signaling.

Crystal structure of the TLR1-TLR2 heterodimer induced by binding of a tri-acylated lipopeptide.,Jin MS, Kim SE, Heo JY, Lee ME, Kim HM, Paik SG, Lee H, Lee JO Cell. 2007 Sep 21;130(6):1071-82. PMID:17889651[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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Citations
282 reviews cite this structure
The role of pattern-recognition receptors in innate immunity: update on Toll-like receptors.
Kawai et al. (2010)
281 more
516 other articles
No citations found

See Also

References

  1. ↑ Kang JY, Nan X, Jin MS, Youn SJ, Ryu YH, Mah S, Han SH, Lee H, Paik SG, Lee JO. Recognition of lipopeptide patterns by Toll-like receptor 2-Toll-like receptor 6 heterodimer. Immunity. 2009 Dec 18;31(6):873-84. PMID:19931471 doi:10.1016/j.immuni.2009.09.018
  2. ↑ Jin MS, Kim SE, Heo JY, Lee ME, Kim HM, Paik SG, Lee H, Lee JO. Crystal structure of the TLR1-TLR2 heterodimer induced by binding of a tri-acylated lipopeptide. Cell. 2007 Sep 21;130(6):1071-82. PMID:17889651 doi:http://dx.doi.org/10.1016/j.cell.2007.09.008

Contents


PDB ID 2z82

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OCA

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