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. 2010 Jun 1;107(24):10990–10995. doi: 10.1073/pnas.1004153107

Fig. 1.

Fig. 1.

cMD-1 structure and sequence. (A) Overall structure of cMD-1 and its hydrophobic cavity. The cMD-1 structure is shown in ribbons that are colored from N terminus (blue) to C terminus (red). Labels for β-strands in sheet-2 are underlined. Disulfide bonds are shown in yellow ball-and-stick models, and a putative PGT molecule inside the MD-1 cavity is shown in sticks (carbon, gray; oxygen, red; phosphorus, orange). (B) MD-1 and MD-2 sequence alignment. cMD-1 cysteine residues that form disulfide bonds are colored in red, and cMD-1 residues that make contacts with lipid IVa are highlighted in yellow. cMD-1 β-strands are shown as arrows above the cMD-1 sequence.