Lipid-polymer nanoparticles to probe the native-like environment of intramembrane rhomboid protease GlpG and its activity

Autor: Henry Sawczyc, Takashi Tatsuta, Carl Öster, Spyridon Kosteletos, Sascha Lange, Claudia Bohg, Thomas Langer, Adam Lange

Publikováno v: Nature Communications, Vol 15, Iss 1, Pp 1-9 (2024)

Abstract Polymers can facilitate detergent-free extraction of membrane proteins into nanodiscs (e.g., SMALPs, DIBMALPs), incorporating both integral membrane proteins as well as co-extracted native membrane lipids. Lipid-only SMALPs and DIBMALPs have

Externí odkaz: https://doaj.org/article/51fe6fabf26f4663ba7e2fcd3c4620ab

Structural Plasticity of the Selectivity Filter in Cation Channels

Autor: Kitty Hendriks, Carl Öster, Adam Lange

Publikováno v: Frontiers in Physiology, Vol 12 (2021)

Ion channels allow for the passage of ions across biological membranes, which is essential for the functioning of a cell. In pore loop channels the selectivity filter (SF) is a conserved sequence that forms a constriction with multiple ion binding si

Externí odkaz: https://doaj.org/article/0d56387b683f4968b8d00504ded494aa

A combination of solid-state NMR and MD simulations reveals the binding mode of a rhomboid protease inhibitor

Autor: Adam Lange, Tillmann Utesch, Susanne Bischoff, Chaowei Shi, Claudia Bohg, Sascha Lange, Han Sun, Carl Öster

Publikováno v: Chemical Science

Intramembrane proteolysis plays a fundamental role in many biological and pathological processes. Intramembrane proteases thus represent promising pharmacological targets, but few selective inhibitors have been identified. This is in contrast to thei

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c56bed5965b92fbccd67fa177032a842
https://doi.org/10.1039/d1sc02146j

Structure and Dynamics of the Rhomboid Protease GlpG in Liposomes Studied by Solid-State NMR

Autor: Carl Öster, Veniamin Chevelkov, Claudia Bohg, Sascha Lange, Chaowei Shi, Adam Lange, Longmei Li

Publikováno v: Journal of the American Chemical Society. 141:17314-17321

Rhomboid proteases are intramembrane proteases that hydrolyze substrate peptide bonds within the lipid bilayer and are important for a wide range of biological processes. The bacterial intramembrane protease GlpG is one of the model systems for struc

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3c95104ed1990b100871339cea224c26
https://doi.org/10.1021/jacs.9b08952

Architecture of the flexible tail tube of bacteriophage SPP1

Autor: Raimond B. G. Ravelli, Adam Lange, Maximilian Zinke, Sophie Zinn-Justin, Michael Habeck, Carl Öster, Katrin A. A. Sachowsky, Gunnar F. Schröder

Publikováno v: Nature Communications, 11(1):5759. Nature Publishing Group
Nature Communications
Nature Communications, 2020, 11 (1), pp.5759. ⟨10.1038/s41467-020-19611-1⟩
Nature Communications, Vol 11, Iss 1, Pp 1-9 (2020)
Nature Communications 11(1), 5759 (2020). doi:10.1038/s41467-020-19611-1
Nature Communications, Nature Publishing Group, 2020, 11 (1), pp.5759. ⟨10.1038/s41467-020-19611-1⟩

Bacteriophage SPP1 is a double-stranded DNA virus of the Siphoviridae family that infects the bacterium Bacillus subtilis. This family of phages features a long, flexible, non-contractile tail that has been difficult to characterize structurally. Her

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::03c847c514cd3b1e72164e706c41a031
https://doi.org/10.1038/s41467-020-19611-1