Els Pardon

TL;DR: This crystal structure represents the first high-resolution view of transmembrane signalling by a GPCR and the most surprising observation is a major displacement of the α-helical domain of Gαs relative to the Ras-like GTPase domain.

TL;DR: A camelid antibody fragment to the human β2 adrenergic receptor is generated, and an agonist-bound, active-state crystal structure of the receptor-nanobody complex is obtained, providing insights into the process of agonist binding and activation.

TL;DR: The structure of an agonist-bound, active state of the human M2 muscarinic acetylcholine receptor stabilized by a G-protein mimetic camelid antibody fragment isolated by conformational selection using yeast surface display reveals larger conformational changes in the extracellular region and orthosteric binding site than observed in the active states of the β2AR and rhodopsin.

TL;DR: A general protocol for the generation of Nanobodies to be used as crystallization chaperones for the structural investigation of diverse conformational states of flexible (membrane) proteins and complexes thereof.

TL;DR: The results give conclusive support to the biochemical finding that the phosphomannomutase deficiency is the basis for CDG1.