Premium
Interaction of a fragment of the cannabinoid CB1 receptor C‐terminus with arrestin‐2
Author(s) -
Bakshi Kunal,
Mercier Richard W.,
Pavlopoulos Spiro
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.09.030
Subject(s) - arrestin , rhodopsin , peptide , chemistry , stereochemistry , receptor , cannabinoid receptor , cannabinoid , desensitization (medicine) , residue (chemistry) , g protein coupled receptor , biophysics , biochemistry , biology , antagonist , retinal
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.