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Interaction of a fragment of the cannabinoid CB1 receptor C-terminus with arrestin-2.

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.

SUBMITTER: Bakshi K

PROVIDER: S-EPMC2151313 | biostudies-literature | 2007 Oct

REPOSITORIES: biostudies-literature

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Interaction of a fragment of the cannabinoid CB1 receptor C-terminus with arrestin-2.

Bakshi Kunal K Mercier Richard W RW Pavlopoulos Spiro S

FEBS letters 20070924 25

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 dipho ...[more]

PMID: 17910957

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2023-12-07 | GSE249503 | GEO

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