2z80

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spinqualitylabelsall models 2z80, resolution 1.8Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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

Overview

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.

About this Structure

2Z80 is a Single protein structure of sequence from Homo sapiens, eptatretus burgeri with as ligand. Full crystallographic information is available from OCA.

Reference

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

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