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. Author manuscript; available in PMC: 2006 Feb 25.

Published in final edited form as: Biochemistry. 2005 Jun 28;44(25):8959–8975. doi: 10.1021/bi047316u

Helical wheel diagrams of G protein-coupled receptors. The helical wheel diagrams show the hydrophobic moment (blue arrow) (42) and helical packing moments (red arrow) (38) for rhodopsin (A), the opsin subfamily (B), the Class A family (C), the Ste2 receptor (D), the Ste2 subfamily (E), and the Ste3 subfamily (F). For panels A–C, the positions are numbered as in bovine rhodopsin; for panels D and E, the positions are numbered as in Ste2, and in panel F, the positions are numbered as in Ste3. The sites that are group-conserved (>80%) across a family or subfamily are colored as follows: small and weakly polar (orange), strongly polar (azure), aromatic (green), and hydrophobic (dark gray). The hydrophobic sites with group conservation between 70% and 80% are light gray. For rhodopsin (A), occluded (solvent inaccessible) and exposed (solvent accessible) residues are indicated by open circles and closed circles, respectively, based on the high-resolution structure. Note that H2 in the Ste2 subfamily (D) has no helical packing moment according to our definition (38). The two strongest moments are shown as thin red arrows.

Helical wheel diagrams of G protein-coupled receptors. The helical wheel diagrams show the hydrophobic moment (blue arrow) (42) and helical packing moments (red arrow) (38) for rhodopsin (A), the opsin subfamily (B), the Class A family (C), the Ste2 receptor (D), the Ste2 subfamily (E), and the Ste3 subfamily (F). For panels A–C, the positions are numbered as in bovine rhodopsin; for panels D and E, the positions are numbered as in Ste2, and in panel F, the positions are numbered as in Ste3. The sites that are group-conserved (>80%) across a family or subfamily are colored as follows: small and weakly polar (orange), strongly polar (azure), aromatic (green), and hydrophobic (dark gray). The hydrophobic sites with group conservation between 70% and 80% are light gray. For rhodopsin (A), occluded (solvent inaccessible) and exposed (solvent accessible) residues are indicated by open circles and closed circles, respectively, based on the high-resolution structure. Note that H2 in the Ste2 subfamily (D) has no helical packing moment according to our definition (38). The two strongest moments are shown as thin red arrows.