[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

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ACS Synthetic Biology
DOI: 10.1021/acssynbio.8b00348
  • Posted in ACS Synthetic Biology, Publications
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[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

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Biochemistry
DOI: 10.1021/acs.biochem.8b01096

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.
  • Posted in Nat Chem Biol, Publications
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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.
  • Posted in Nat Chem Biol, Publications
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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.
  • Posted in Nat Chem Biol, Publications
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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.
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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.
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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
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[ASAP] Ancient Family of Retinal Proteins Brought to Light “Sight-Unseen”

November 30th, 2018 by Thomas P. Sakmar, Thomas Huber

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Biochemistry
DOI: 10.1021/acs.biochem.8b01188