Helix Formation in Arrestin Accompanies Recognition of Photoactivated Rhodopsin
| Autor: | Rudolf Hartmann, Oliver P. Ernst, Matthias Stoldt, Joachim Granzin, Peter Henklein, Bernd W. Koenig, Dieter Willbold, Martin Heck, Sophie Feuerstein, Alexander Pulvermüller |
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| Rok vydání: | 2009 |
| Předmět: |
Models
Molecular chemistry.chemical_classification Rhodopsin Arrestin genetic structures Photochemistry Protein Conformation Peptide ROD ARRESTIN Biology Biochemistry eye diseases chemistry Helix Biophysics biology.protein Arrestin beta 2 Phosphorylation Arrestin beta 1 sense organs Nuclear Magnetic Resonance Biomolecular |
| Zdroj: | Biochemistry. 48:10733-10742 |
| ISSN: | 1520-4995 0006-2960 |
| Popis: | Binding of arrestin to photoactivated phosphorylated rhodopsin terminates the amplification of visual signals in photoreceptor cells. Currently, there is no crystal structure of a rhodopsin-arrestin complex available, although structures of unbound rhodopsin and arrestin have been determined. High-affinity receptor binding is dependent on distinct arrestin sites responsible for recognition of rhodopsin activation and phosphorylation. The loop connecting beta-strands V and VI in rod arrestin has been implicated in the recognition of active rhodopsin. We report the structure of receptor-bound arrestin peptide Arr(67-77) mimicking this loop based on solution NMR data. The peptide binds photoactivated rhodopsin in the unphosphorylated and phosphorylated form with similar affinities and stabilizes the metarhodopsin II photointermediate. A largely alpha-helical conformation of the receptor-bound peptide is observed. |
| Databáze: | OpenAIRE |
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