Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2050800 | FEBS Letters | 2007 | 8 Pages |
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.
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Authors
Kunal Bakshi, Richard W. Mercier, Spiro Pavlopoulos,