Table 2.
Cholesterol-binding residues in β2-adrenergic receptor structures (PDB ID: 2RH1 and 3D4S).
| Residue | 2RH1 | 3D4S | ω-ratio |
|---|---|---|---|
| Val 48 | + | − | 0.024 |
| Phe 49 | + | − | 0.019 |
| Val 52 | + | − | 0.122 |
| Ile 55 | + | + | 0.022 |
| Ala 59 | − | + | 0.334 |
| Tyr 70* | − | + | 0.424 |
| Thr 73 | − | + | 0.114 |
| Ser 74 | − | + | 0.026 |
| Cys 77 | + | + | 0.022 |
| Leu 80 | + | + | 0.032 |
| Val 81 | + | + | 0.117 |
| Leu 84 | + | + | 0.030 |
| Ala 85 | − | + | 0.621 |
| Phe 108 | + | − | 0.019 |
| Ile 112 | + | + | 0.528 |
| Leu 115 | − | + | 0.029 |
| Arg 151* | − | + | 0.134 |
| Ile 154* | + | + | 0.112 |
| Leu 155 | + | − | 0.169 |
| Trp 158* | + | + | 0.024 |
| Leu 339 | + | − | 0.114 |
*
Residues in the cholesterol consensus motif (CCM)
Residues under the strongest purifying selection are shown in bold; “+” or “−“ signs indicate whether the residue interacts (“+”) or does not interact (“−“) with cholesterol.