Fig. 4: Structural features of ligand binding pocket of GPR109A. | Nature Communications

Fig. 4: Structural features of ligand binding pocket of GPR109A.

From: Structure-guided engineering of biased-agonism in the human niacin receptor via single amino acid substitution

Fig. 4

a, b Structural features of ligand (MK6892) bound-GPR109A, N-terminal β-hairpin, close-up view of ECL2 dipping into the orthosteric pocket and ribbon diagram of disulfide bridges formed at the ligand binding pocket. c Superposed niacin, acipimox, MK6892, GSK256073 and MMF bound GPR109A structures highlighting the orthosteric binding pocket (cross-sections of GPR109A bound to the individual ligand). d GPR109A ligand binding pocket highlighting the major interactions of the individual ligand (black dotted line represents H-bond and ionic interactions).

Back to article page