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

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• 作者：Kunal Bakshi ; Richard W. Mercier ; Spiro Pavlopoulos
• 关键词：Arrestin ; CB1 ; C-terminus ; Complex ; Phosphorylation ; NMR
• 刊名：FEBS Letters
• 出版年：2007
• 出版时间：16 October 2007
• 年：2007
• 卷：581
• 期：25
• 页码：5009-5016
• 全文大小：676 K

文摘

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.