Fig. 2
Trimers of Mag-2 dimers form a hexameric structure with the hydrophobic interface exposed towards the membrane and a positively charged channel facing inward. (A) The hexameric Mag-2 channel structure depicted in cartoon representation, assembled via trimerization of dimers (NT: N-terminus, CT: C-terminus). Two orientations of the structure are shown as top and side-view related to each other by a rotation of 90 degrees around the X-axis. One of the dimers forms a wall-like structure facing the membrane surrounding it. (B) Surface representation of the two hexameric structures shown in the same orientation as (A) and color-coded based on the amino acid residual properties. Hydrophobic residues are colored in green, positively charged residues are blue and negatively charged residues are red and amphiphilic residues in magenta.
