James Barwell

TL;DR: A review of the key roles of extracellular loops in ligand binding, activation and regulation of both family A and family B GPCRs is presented in this article, with a focus on the role of ECL segments.

TL;DR: The structures and accompanying pharmacology data reveal how a class of accessory membrane proteins modulate ligand binding of a GPCR and may inform drug development targeting CLR:RAMP complexes.

TL;DR: The interaction of RAMPs with the glucagon‐like peptide 1 receptor (GLP‐1 receptor), the human vasoactive intestinal polypeptide/pituitary AC‐activating peptide 2 receptor (VPAC2) and the type 1 corticotrophin releasing factor receptor (CRF1) has been examined.

TL;DR: This review encapsulates current thinking in the realm of family B GPCR research by highlighting both conflicting and recurring themes and how such findings relate to two unusual but important receptors, CTR and CLR.

TL;DR: The variation of sequence variability with structure, the analysis of polarity violations, the alignment of group-conserved residues and the mutagenesis results at 27 key positions were particularly informative in distinguishing between the proposed and plausible alternative alignments.