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Structural features of activated GPCR signaling complexes
G protein-coupled receptors (GPCRs) couple to diverse heterotrimeric G protein subtypes and then activate downstream signaling pathways in classical GPCR activation. It has also been found that GPCRs transduce signals through different regulatory proteins, such as arrestins. Recently, owing to the b...
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Published in: | Current opinion in structural biology 2020-08, Vol.63, p.82-89 |
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Main Authors: | , , |
Format: | Article |
Language: | English |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | G protein-coupled receptors (GPCRs) couple to diverse heterotrimeric G protein subtypes and then activate downstream signaling pathways in classical GPCR activation. It has also been found that GPCRs transduce signals through different regulatory proteins, such as arrestins. Recently, owing to the breakthroughs in cryo-electron macroscopy (Cryo-EM), numerous structures of GPCR-G protein or GPCR-arrestin complexes have been deciphered. In this review, we summarize most of reported GPCR signaling complex structures, with an emphasis on the structural features of rhodopsin-like GPCR activation and G protein-binding/arrestin-binding modes, to illustrate the activation and signaling mechanism of rhodopsin-like GPCRs. |
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ISSN: | 0959-440X 1879-033X |
DOI: | 10.1016/j.sbi.2020.04.008 |