[ASAP] Structure-Based Design of Versatile Biosensors for Small Molecules Based on the PAS Domain of a Thermophilic Histidine Kinase
December 10th, 2018 by Kai U. Cormann, Meike Baumgart, Michael Bott
[ASAP] Mechanistic Characterization of Long Residence Time Inhibitors of Diacylglycerol Acyltransferase 2 (DGAT2)
December 7th, 2018 by Brandon Pabst, Kentaro Futatsugi, Qifang Li, Kay Ahn
Programmable and printable <i>Bacillus subtilis</i> biofilms as engineered living materials
December 3rd, 2018 by Jiaofang Huang
Programmable and printable Bacillus subtilis biofilms as engineered living materials
Programmable and printable <i>Bacillus subtilis</i> biofilms as engineered living materials, Published online: 03 December 2018; doi:10.1038/s41589-018-0169-2
Co-opting the amyloid machinery from Bacillus subtilis, engineering of TasA fusion proteins enables the assembly of functionalized biofilms with tunable physicochemical properties that are amenable to 3D printing and microencapsulation techniques.Crystal structure of misoprostol bound to the labor inducer prostaglandin E<sub>2</sub> receptor
December 3rd, 2018 by Martin Audet
Crystal structure of misoprostol bound to the labor inducer prostaglandin E2 receptor
Crystal structure of misoprostol bound to the labor inducer prostaglandin E<sub>2</sub> receptor, Published online: 03 December 2018; doi:10.1038/s41589-018-0160-y
A structure of the prostaglandin E2 receptor 3 (EP3) bound to the agonist misoprostol shows a completely enclosed binding pocket with a structured water molecule that coordinates misoprostol's ring structure and explains the receptor's selectivity.Structures shed light on prostanoid signaling
December 3rd, 2018 by Kaspar Hollenstein
Structures shed light on prostanoid signaling
Structures shed light on prostanoid signaling, Published online: 03 December 2018; doi:10.1038/s41589-018-0178-1
Prostanoids signal through G-protein-coupled receptors to regulate diverse physiological processes. Structures of three prostanoid receptors in inactive and active conformations now uncover the molecular determinants of ligand recognition and receptor activation and offer new opportunities for drug discovery.Crystal structure of the endogenous agonist-bound prostanoid receptor EP3
December 3rd, 2018 by Kazushi Morimoto
Crystal structure of the endogenous agonist-bound prostanoid receptor EP3
Crystal structure of the endogenous agonist-bound prostanoid receptor EP3, Published online: 03 December 2018; doi:10.1038/s41589-018-0171-8
Structural analysis of prostaglandin E receptor EP3, a member of the prostanoid receptor subfamily of GPCRs, in complex with the endogenous agonist PGE2 reveals important interactions and motions required for receptor activation.Structural basis for ligand recognition of the human thromboxane A<sub>2</sub> receptor
December 3rd, 2018 by Hengxin Fan
Structural basis for ligand recognition of the human thromboxane A2 receptor
Structural basis for ligand recognition of the human thromboxane A<sub>2</sub> receptor, Published online: 03 December 2018; doi:10.1038/s41589-018-0170-9
Structures of the human thromboxane A2 receptor, a member of the prostanoid family of G-protein-coupled receptors, in complex with two synthetic antagonists reveal that ligands access the ligand-binding pocket from the plane of the lipid bilayer.Ligand binding to human prostaglandin E receptor EP<sub>4</sub> at the lipid-bilayer interface
December 3rd, 2018 by Yosuke Toyoda
Ligand binding to human prostaglandin E receptor EP4 at the lipid-bilayer interface
Ligand binding to human prostaglandin E receptor EP<sub>4</sub> at the lipid-bilayer interface, Published online: 03 December 2018; doi:10.1038/s41589-018-0131-3
The structure of human prostaglandin E receptor EP4 in complex with antagonist ONO-AE3-208 and a functional antibody reveals a ligand-binding site at the interface of the lipid bilayer that is unique among GPCRs.Publisher Correction: Structural insights into binding specificity, efficacy and bias of a β<sub>2</sub>AR partial agonist
November 30th, 2018 by Matthieu Masureel
Publisher Correction: Structural insights into binding specificity, efficacy and bias of a β2AR partial agonist
Publisher Correction: Structural insights into binding specificity, efficacy and bias of a β<sub>2</sub>AR partial agonist, Published online: 30 November 2018; doi:10.1038/s41589-018-0182-5
Publisher Correction: Structural insights into binding specificity, efficacy and bias of a β2AR partial agonist[ASAP] Ancient Family of Retinal Proteins Brought to Light “Sight-Unseen”
November 30th, 2018 by Thomas P. Sakmar, Thomas Huber
