Markus Koglin

TL;DR: A completely novel allosteric binding site for class B receptors is described, providing an opportunity for structure-based drug design for this receptor class and furthering the understanding of the mechanisms of activation of these receptors.

TL;DR: A number of new developments in over-expressing receptors, as well as formulating stable pure protein, are contributing to the growing interest in targeting GPCRs with antibodies.

TL;DR: Biophysical fragment screening of a thermostabilized β1-adrenergic receptor (β1AR) using surface plasmon resonance (SPR) enabled the identification of moderate affinity, high ligand efficiency (LE) arylpiperazine hits 7 and 8, and a structure-based design approach using protein–ligand crystal structures of the β1AR resulted in several fragments that bound with higher affinity.

TL;DR: The progress made by targeting GPCRs with antibody-based therapeutics, as well as technical hurdles to overcome, are presented and discussed in this Review.

TL;DR: The structure demonstrates that NDT9513727 exerts its inverse-agonist activity through an extra-helical mode of action, and is a non-peptide inverse agonist of C5aR1, which is highly selective for the primate and gerbil receptors over those of other species.