David T. Lodowski

TL;DR: Rhodopsins found in Eukaryotes, Bacteria, and Archaea consist of opsin apoproteins and a covalently linked retinal which is employed to absorb photons for energy conversion or the initiation of intra- or intercellular signaling.

TL;DR: In this paper, the crystal structures of both ground state and a photoactivated deprotonated intermediate of bovine rhodopsin at a resolution of 4.15 A were reported.

TL;DR: Supporting by structure-activity relationship information arising from empirical screening, a unified structural model of GPCR activation/inactivation promises to both accelerate drug discovery in this field and improve the fundamental understanding of structure-based drug design in general.

TL;DR: The structure of full-length TRPV2 is determined at ∼5 Å resolution by cryo-electron microscopy and contains two constrictions, one each in the pore-forming upper and lower gates, which are proposed to contribute to diversity ofTRPV channels.

TL;DR: This work uses time-resolved structural mass spectrometry techniques to investigate GPCR-G protein complex formation and G-protein activation and suggests that coupling specificity is determined by one or more transient intermediate states that serve as selectivity filters and precede the formation of the stable nucleotide-free GPCG protein complexes observed in crystal and cryo-EM structures.