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

被引:30
作者
Bakshi, Kunal [1 ]
Mercier, Richard W. [1 ]
Pavlopoulos, Spiro [1 ]
机构
[1] Univ Connecticut, Dept Pharmaceut Sci, Ctr Drug Discovery, Storrs, CT 06269 USA
关键词
arrestin; CB1; C-terminus; complex; phosphorylation; NMR;
D O I
10.1016/j.febslet.2007.09.030
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Desensitization of the cannabinoid CBI 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 CBI C-terminus upon binding to arrestin-2. This segment is pivotal to the desensitization of CBI. 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. (c) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
引用
收藏
页码:5009 / 5016
页数:8
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