Table 1.
Alignment of hydrophobic pocket residues for select GPCRs.
| GPCR | ECL2-TM5 Sequence* | ||||||
|---|---|---|---|---|---|---|---|
| 45.52 | 5.35 | 5.36 | 5.37 | 5.38 | 5.39 | 5.40 | |
| D1R | Ser | Ser | Arg | Thr | Tyr | Ala | Ile |
| D2R | Ile | Asn | Pro | Ala | Phe | Val | Val |
| D3R | Ile | Asn | Pro | Asp | Phe | Val | Ile |
| D4R | Leu | Asp | Arg | Asp | Tyr | Val | Val |
| D5R | Ser | Asn | Arg | Thr | Tyr | Ala | Ile |
| 5-HT1AR | Ile | Asp | His | Gly | Tyr | Thr | Ile |
| 5-HT1BR | Val | His | Ile | Lys | Tyr | Thr | Val |
| 5-HT2AR | Leu | Asp | Asp | Asn | Phe | Val | Leu |
| 5-HT2BR | Leu | Phe | Gly | Asp | Phe | Met | Leu |
| 5-HT2CR | Leu | Asp | Pro | Asn | Phe | Val | Leu |
| ⍺1A | Ile | Glu | Pro | Gly | Tyr | Val | Leu |
| ⍺1B | Val | Glu | Pro | Phe | Tyr | Ala | Leu |
| ⍺1D | Ile | Glu | Ala | Gly | Tyr | Ala | Val |
| ⍺2A | Ile | Gln | Lys | Trp | Tyr | Val | Ile |
| ⍺2B | Leu | Glu | Ala | Trp | Tyr | Ile | Leu |
| ⍺2C | Leu | Glu | Thr | Trp | Tyr | Ile | Leu |
| β1R | Phe | Gln | Arg | Ala | Tyr | Ala | Ile |
| β2R | Phe | Gln | Gln | Ala | Tyr | Ala | Ile |
| β3R | Phe | Gln | Met | Pro | Tyr | Val | Leu |
| V2R | Ala | Arg | Arg | Thr | Tyr | Val | Thr |
Amino acid positions in transmembrane (TM) regions are delineated using Ballesteros and Weinstein nomenclature (29). The amino acid position in extracellular loop 2 (EL2) is delineated using the nomenclature developed by de Graaf et al. (77). Yellow indicates nonpolar amino acids with an aliphatic group (Ala, Val, Ile, Leu, Met, Gly); light green indicates hydrophobic amino acids with an aromatic ring (Phe, Tyr); dark green indicates Trp; purple indicates polar amino acids with an uncharged side chain (Ser, Thr, Asn, Gln); light grey indicates Pro; red indicates negatively charged amino acids (Glu, Asp); blue indicates positively charged amino acids (Arg, His, Lys).