Structural and Biophysical Mechanisms of Class C G Protein-Coupled Receptor Function.
Structural and Biophysical Mechanisms of Class C G Protein-Coupled Receptor Function.
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DOI:
10.1016/j.tibs.2020.07.008
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发表时间:
2020-12
影响因子:
13.8
通讯作者:
Levitz J
中科院分区:
文献类型:
--
作者:
Ellaithy A;Gonzalez-Maeso J;Logothetis DA;Levitz J
Groundbreaking structural and spectroscopic studies of class A G protein-coupled receptors (GPCRs), such as rhodopsin and the β2 adrenergic receptor, have provided a picture of how structural rearrangements between transmembrane helices control ligand binding, receptor activation and effector coupling. However, the activation mechanism of other GPCR classes remains more elusive in large part due to complexity in their domain assembly and quaternary structure. In this review, we focus on the class C GPCRs, which includes metabotropic glutamate receptors (mGluRs) and gamma-aminobutyric acid B (GABAB) receptors most prominently. We discuss the unique biophysical questions raised by the presence of large extracellular ligand binding domains (LBD) and constitutive homo/hetero-dimerization. Furthermore, we discuss how recent studies have begun to unravel how these fundamental class C GPCR features impact the processes of ligand binding, receptor activation, signal transduction, regulation by accessory proteins and crosstalk with other GPCRs.
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