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. Author manuscript; available in PMC: 2020 Aug 4.
Published in final edited form as: Sci Signal. 2020 Feb 4;13(617):eaaw5885. doi: 10.1126/scisignal.aaw5885

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).