Key residues in TLR4-MD2 tetramer formation identified by free energy simulations
Fig 2
The structure of mouse MD2 in the lipopolysaccharide (LPS)-bound (TLR4-MD2)2 tetramer complex.
a) The residue sequences of MD2 and the residues within secondary structures of β-sheet and helix are colored in yellow and cyan shadow respectively. The C strand in the neoseptin3-bound complex starts at residue S45. In the ligand-free complex: the A strand ends at S27, the C strand starts at S45, the D strand starts at T57, the F and G strands are combined together as one strand (i.e., I85 to V93), the H strand ends at F121, and the I strand starts at C133. b) The three-dimensional crystal structure of MD2. The secondary structures of β-sheet and helix are colored in yellow and cyan respectively.