%0 Journal Article
%A Feuerstein, S.E.
%A Pulvermüller, A.
%A Hartmann, R.
%A Granzin, J.
%A Stoldt, M.
%A Henklein, P.
%A Ernst, O.P.
%A Heck, M.
%A Willbold, D.
%A Koenig, B. W.
%T Helix Formation in Arrestin Accompanies Recognition of Photoactivated Rhodopsin
%J Biochemistry
%V 48
%@ 0006-2960
%C Columbus, Ohio
%I American Chemical Society
%M PreJuSER-7146
%P 10733  -10742
%D 2009
%Z 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).
%X 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.
%K Arrestin: chemistry
%K Models, Molecular
%K Nuclear Magnetic Resonance, Biomolecular
%K Photochemistry
%K Protein Conformation
%K Rhodopsin: chemistry
%K Arrestin (NLM Chemicals)
%K Rhodopsin (NLM Chemicals)
%K J (WoSType)
%F PUB:(DE-HGF)16
%9 Journal Article
%$ pmid:19835414
%U <Go to ISI:>//WOS:000271459100009
%R 10.1021/bi900544p
%U https://juser.fz-juelich.de/record/7146