Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
8320039 | Current Opinion in Structural Biology | 2014 | 9 Pages |
Abstract
- Novel structures provide insight into the arrestin activation mechanism.
- Arrestins are pre-activated by a C-tail exchange mechanism.
- Functional data for arrestin-1 are largely transferable to other arrestin subtypes.
- Three clusters of conserved phosphate sensors establish high affinity interactions.
- Arrestins provide tunable phosphate sensors for differentially phosphorylated GPCRs.
Related Topics
Life Sciences
Biochemistry, Genetics and Molecular Biology
Biochemistry
Authors
Martin K Ostermaier, Gebhard FX Schertler, Joerg Standfuss,