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Structural basis of ligand selectivity and disease mutations in cysteinyl leukotriene receptors
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Structural basis of ligand selectivity and disease mutations in cysteinyl leukotriene receptors
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Journal Article
Structural basis of ligand selectivity and disease mutations in cysteinyl leukotriene receptors
2019
Overview
Cysteinyl leukotriene G protein-coupled receptors CysLT
1
and CysLT
2
regulate pro-inflammatory responses associated with allergic disorders. While selective inhibition of CysLT
1
R has been used for treating asthma and associated diseases for over two decades, CysLT
2
R has recently started to emerge as a potential drug target against atopic asthma, brain injury and central nervous system disorders, as well as several types of cancer. Here, we describe four crystal structures of CysLT
2
R in complex with three dual CysLT
1
R/CysLT
2
R antagonists. The reported structures together with the results of comprehensive mutagenesis and computer modeling studies shed light on molecular determinants of CysLTR ligand selectivity and specific effects of disease-related single nucleotide variants.
Cysteinyl leukotriene G protein-coupled receptors CysLT
1
and CysLT
2
regulate pro-inflammatory responses associated with allergic disorders. Here, authors describe four crystal structures of CysLT
2
R in complex with three dual CysLT
1
R/CysLT
2
R antagonists, which shed light on CysLTR ligand selectivity.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 13/109
/ 13/31
/ 13/44
/ 13/95
/ 82/16
/ 82/29
/ 82/80
/ 82/83
/ Animals
/ Asthma
/ Atopy
/ Humanities and Social Sciences
/ Humans
/ Ligands
/ Molecular Docking Simulation
/ Mutation
/ Receptors, Leukotriene - chemistry
/ Receptors, Leukotriene - drug effects
/ Receptors, Leukotriene - genetics
/ Science
