西亚试剂：Crystal Structure of the TLR1-TLR2 Heterodimer Induced by B

Crystal Structure of the TLR1-TLR2 Heterodimer Induced by Binding of a Tri-Acylated Lipopeptide

Mi Sun Jin,1 Sung Eun Kim,1,4 Jin Young Heo,1,4 Mi Eun Lee,1 Ho Min Kim,1 Sang-Gi Paik,3 Hayyoung Lee,3 and Jie-Oh Lee1,2,

1 Department of Chemistry, Korea Advanced Institute of Science and Technology, Daejon, Korea 305-701
2 Institute for Bio-Century, Korea Advanced Institute of Science and Technology, Daejon, Korea 305-701
3 Department of Biology, School of Bioscience & Biotechnology, Chungnam National University, Daejon, Korea 305-764

Corresponding author
Jie-Oh Lee
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, Pam3CSK4, induced the formation of an “m” shaped heterodimer of the TLR1 and TLR2 ectodomains whereas binding of the di-acylated lipopeptide, Pam2CSK4, did not. The three lipid chains of Pam3CSK4 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.

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