Journal Article

PreJuSER-7146

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Helix Formation in Arrestin Accompanies Recognition of Photoactivated Rhodopsin

Feuerstein, S. E.FZJ* ; Pulvermüller, A. ; Hartmann, R.FZJ* ; Granzin, J.FZJ* ; Stoldt, M.FZJ* ; Henklein, P. ; Ernst, O. P. ; Heck, M. ; Willbold, D.FZJ* ; Koenig, B. W.FZJ*

2009
American Chemical Society Columbus, Ohio

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Please use a persistent id in citations: doi:10.1021/bi900544p

Abstract: 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.

Keyword(s): Arrestin: chemistry (MeSH) ; Models, Molecular (MeSH) ; Nuclear Magnetic Resonance, Biomolecular (MeSH) ; Photochemistry (MeSH) ; Protein Conformation (MeSH) ; Rhodopsin: chemistry (MeSH) ; Arrestin ; Rhodopsin ; J

Note: This work was supported by grants from the Deutsche Forschungsgemeinschaft (DFG) to B.W.K. (Ko 2143/3), AR (Pu 186/3), and O.P. E. (Er 294/1).

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Contributing Institute(s):

1. Strukturbiochemie (ISB-3)

Research Program(s):

1. Funktion und Dysfunktion des Nervensystems (P33)

Appears in the scientific report 2010

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