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- W2007102702 abstract "The mammalian dim-light photoreceptor rhodopsin is a prototypic G protein coupled receptor (GPCR), interacting with the G protein, transducin, rhodopsin kinase, and arrestin. All of these proteins interact with rhodopsin at its cytoplasmic surface. Structural and modeling studies have provided in-depth descriptions of the respective interfaces. Overlap and thus competition for binding surfaces is a major regulatory mechanism for signal processing. Recently, it was found that the same surface is also targeted by small molecules. These ligands can directly interfere with the binding and activation of the proteins of the signal transduction cascade, but they can also allosterically modulate the retinal ligand binding pocket. Because the pocket that is targeted contains residues that are highly conserved across Class A GPCRs, these findings imply that it may be possible to target multiple GPCRs with the same ligand(s). This is desirable for example in complex diseases such as cancer where multiple GPCRs participate in the disease networks. Keywords: G protein coupled receptors, allostery, conformational changes, docking, protein-protein interactions, Rhodopsin, drug discovery, cytoplasm, GPCR, crystal structure" @default.
- W2007102702 created "2016-06-24" @default.
- W2007102702 creator A5014665461 @default.
- W2007102702 creator A5022944167 @default.
- W2007102702 creator A5030348396 @default.
- W2007102702 creator A5065265042 @default.
- W2007102702 date "2012-01-01" @default.
- W2007102702 modified "2023-09-27" @default.
- W2007102702 title "The Cytoplasmic Rhodopsin-Protein Interface: Potential for Drug Discovery" @default.
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- W2007102702 doi "https://doi.org/10.2174/138945012798868461" @default.