Structural features of the apelin receptor N-terminal tail and first transmembrane segment implicated in ligand binding and receptor trafficking

► We present the structure of the N-terminal portion of the human apelin receptor (AR). ► Combining NMR data and MD simulation, we place this in the full-length AR context. ► The first transmembrane helix of AR is a kinked helix and is required for trafficking. ► The AR N-terminal tail has an anionic surface ideal for binding its ligand, apelin. ► This is one of the first structural characterizations of a peptide-activated GPCR.