Tethered peptide activation mechanism of the adhesion GPCRs ADGRG2 and ADGRG4.

Adhesion G protein-coupled receptors (aGPCRs) constitute an evolutionarily ancient family of receptors that often undergo autoproteolysis to produce α and β subunits. A tethered agonism mediated by the 'Stachel sequence' of the β subunit has been proposed to have central roles in aGPCR activation. Here we present three cryo-electron microscopy structures of aGPCRs coupled to the G heterotrimer.

Ligand recognition and allosteric regulation of DRD1-Gs signaling complexes.

Dopamine receptors, including D1- and D2-like receptors, are important therapeutic targets in a variety of neurological syndromes, as well as cardiovascular and kidney diseases. Here, we present five cryoelectron microscopy (cryo-EM) structures of the dopamine D1 receptor (DRD1) coupled to Gs heterotrimer in complex with three catechol-based agonists, a non-catechol agonist, and a positive allosteric modulator for endogenous dopamine. These structures revealed that a polar interaction network is essential for catecholamine-like agonist recognition, whereas specific motifs in the extended binding pocket were responsible for discriminating D1- from D2-like receptors.

Characteristics and Implications of Nanocoatings on Gouges in a Seismically Active Fault Zone.

Using a ZEISS Axio Scope A1 ordinary polarizing microscope, a ZEISS Sigma 300 scanning electron microscope and a HITACHI S4800 scanning electron microscope, we observe micro/nanocharacteristics of slip planes in gouges sampled from the Tanlu fault zone, the Haiyuan fault zone and several other Late Pleistocene active faults, such as the Haiyang fault, the Shuangshan-Lijiazhuang fault and the Xintai-Mengyin fault, in Shandong Province. Based on microscopic observation of gouges, a straight slip zone is a sign of seismic stick slipping. According to scanning electron microscopy results, the surface of gouges is commonly covered by nanocoatings.