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

Article ID	Journal	Published Year	Pages	File Type
10797233	Biochimica et Biophysica Acta (BBA) - Biomembranes	2013	13 Pages	PDF

Abstract

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

Keywords

CSI NOESY HEK NOE PDB RMSD TOCSY DTT IPTG DSS DPPC ERK TFA HSQC DPC FBS DMEM GPCR PEI nuclear magnetic resonance BSA Dulbecco's modified Eagle Medium G-protein coupled receptor bovine serum albumin Trifluoracetic acid isopropyl β-D-1-thiogalactopyranoside NMR Divide and conquer nuclear Overhauser enhancement Dodecylphosphocholine Molecular dynamics dipalmitoylphosphatidylcholine Membrane protein structure sodium 2,2-dimethyl-2-silapentane-5-sulfonate fetal bovine serum chemical shift index Molecular dynamics simulations NOE spectroscopy Total correlation spectroscopy transmembrane Luria broth Homology model root mean square deviation hemagglutinin polymerase chain reaction PCR Protein Data Bank Polyethylenimine human embryonic kidney extracellular signal-regulated kinase apelin receptor heteronuclear single quantum coherence