کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5510841 | 1539335 | 2017 | 10 صفحه PDF | دانلود رایگان |
- Recent crystal structures indicate how arrestin is activated for GPCR binding.
- Multiple binding sites for phosphorylated receptor C-terminus exist on arrestin.
- Interdomain rotation and finger loop flexibility allow arrestin binding to receptor.
- Arrestin and G protein share common binding crevice on the receptor.
- Arrestin C-edge functions as membrane anchor.
The large and multifunctional family of G protein-coupled receptors (GPCRs) are regulated by a small family of structurally conserved arrestin proteins. In order to bind an active GPCR, arrestin must first be activated by interaction with the phosphorylated receptor C-terminus. Recent years have witnessed major developments in high-resolution crystal structures of pre-active arrestins and arrestin or arrestin-derived peptides in complex with an active GPCR. Although each structure individually offers only a limited snapshot, taken together and interpreted in light of recent complementary functional data, they offer valuable insight into how arrestin is activated by and couples to a phosphorylated active GPCR.
Journal: Current Opinion in Structural Biology - Volume 45, August 2017, Pages 160-169