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• W1976573721 abstract "Desensitization of the cannabinoid CB1 receptor is mediated by the interaction with arrestin. In this study, we report the structural changes of a synthetic diphosphorylated peptide corresponding to residues 419–439 of the CB1 C-terminus upon binding to arrestin-2. This segment is pivotal to the desensitization of CB1. Using high-resolution proton NMR, we observe two helical segments in the bound peptide that are separated by the presence a glycine residue. The binding we observe is with a diphoshorylated peptide, whereas a previous study reported binding of a highly phosphorylated rhodopsin fragment to visual arrestin. The arrestin bound conformations of the peptides are compared." @default.
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• W1976573721 date "2007-09-24" @default.
• W1976573721 modified "2023-09-27" @default.
• W1976573721 title "Interaction of a fragment of the cannabinoid CB1 receptor C-terminus with arrestin-2" @default.
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• W1976573721 doi "https://doi.org/10.1016/j.febslet.2007.09.030" @default.
• W1976573721 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2151313" @default.
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