학술논문
Structural studies of phosphorylation-dependent interactions between the V2R receptor and arrestin-2
Document Type
article
Author
Source
Nature Communications, Vol 12, Iss 1, Pp 1-16 (2021)
Subject
Language
English
ISSN
2041-1723
Abstract
The interaction between a GPCR, such as the vasopressin receptor-2 (V2R), and arrestin depends on the receptors’ phosphorylation pattern. Here authors use FRET and NMR to analyze the phosphorylation patterns of the V2R-arrestin complex and show that phospho-interactions are the key determinants of selective arrestin conformational states and correlated functions.