Structural basis of ligand selectivity and disease mutations in cysteinyl leukotriene receptors

Structural basis of ligand selectivity and disease mutations in cysteinyl leukotriene receptors

Cysteinyl leukotriene G protein-coupled receptors CysLT1 and CysLT2 regulate pro-inflammatory responses associated with allergic disorders. Here, authors describe four crystal structures of CysLT2R in complex with three dual CysLT1R/CysLT2R antagonists, which shed light on CysLTR ligand selectivity.

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Detalles Bibliográficos
Autores principales: Anastasiia Gusach, Aleksandra Luginina, Egor Marin, Rebecca L. Brouillette, Élie Besserer-Offroy, Jean-Michel Longpré, Andrii Ishchenko, Petr Popov, Nilkanth Patel, Taku Fujimoto, Toru Maruyama, Benjamin Stauch, Margarita Ergasheva, Daria Romanovskaia, Anastasiia Stepko, Kirill Kovalev, Mikhail Shevtsov, Valentin Gordeliy, Gye Won Han, Vsevolod Katritch, Valentin Borshchevskiy, Philippe Sarret, Alexey Mishin, Vadim Cherezov
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2019
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Science
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Acceso en línea:https://doaj.org/article/c54160b2896f4e3f9bcd8053dc21a8c7
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Sumario:Cysteinyl leukotriene G protein-coupled receptors CysLT1 and CysLT2 regulate pro-inflammatory responses associated with allergic disorders. Here, authors describe four crystal structures of CysLT2R in complex with three dual CysLT1R/CysLT2R antagonists, which shed light on CysLTR ligand selectivity.

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