Fig. 4: The crystal structure of the apelin receptor NxStaR in complex with CMF-019 reveals deep engagement with lipophilic sub-pockets at the bottom of the orthosteric site. | Nature Communications

Fig. 4: The crystal structure of the apelin receptor NxStaR in complex with CMF-019 reveals deep engagement with lipophilic sub-pockets at the bottom of the orthosteric site.

From: Structural and functional determination of peptide versus small molecule ligand binding at the apelin receptor

Fig. 4

a Cartoon representation (rainbow colours) of human apelin stabilised receptor (NxStaR) crystal structure (ICL3 bRIL fusion was omitted for clarity), with the CMF-019 ligand represented as spheres, and oleic acid as sticks. b Close-up view of the CMF-019 binding pose at the bottom of the apelin receptor orthosteric site, with lining amino acids and oleic acid represented as sticks (left), and CMF-019 binding pocket represented as a light grey mesh, with lipophilic hotspots coloured in pale wheat (right). The extracellular vestibule is labelled as ECV, and the lipophilic sub-pockets are labelled as I, II and III. The small table below panel b lists the residues interacting with CMF-019 and the corresponding sub-pockets they line.

Back to article page