Fig. 3: Atomic structures of DLAM5 bound to hTLR4/MD-2 and mTLR4/MD-2, revealing species-independent binding modes.
From: Structural insight into TLR4/MD-2 activation by synthetic LPS mimetics with distinct binding modes
The detailed interactions of DLAM5 with hTLR4/MD-2 (a) and mTLR4/MD-2 (b) complexes. The interactions of DLAM5 are marked by red (electrostatic interaction) and black (hydrophobic interaction) dashed lines. c Superimposition of DLAM5 bound to h- and mTLR4/MD-2. The distances between lipid chain tips are indicated as a–c. d Comparison of the distribution of hydrophobic residues in human and mouse MD-2 pockets, highlighting their contribution to the conformational variability and lipid chain orientation in DLAM5. The disaccharide moiety and overlapped chains of DLAM5 (R2′, and R6) were omitted. e The detailed interactions between hTLR4/MD-2 and lipid A portion of LPS in hTLR4/MD-2/Ra-LPS complex (PDB: 3FXI) f The detailed interactions between mTLR4/MD-2 and lipid A portion of LPS in mTLR4/MD-2/Re-LPS complex (PDB: 3VQ2). Only the lipid A portion is shown for clarity. Superimposition of DLAM5 and E. coli lipid A bound to hTLR4/MD-2 (g) and to mTLR4/MD-2 (h). The colors of DLAM5 and TLR4/MD-2 are consistent with Fig. 2c.
