Description: Helix Formation in Arrestin Accompanies Recognition of Photoactivated Rhodopsin

This title appears in the Scientific Report : 2010

Helix Formation in Arrestin Accompanies Recognition of Photoactivated Rhodopsin

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-a...

Personal Name(s):	Feuerstein, S.E.
	Pulvermüller, A. / Hartmann, R. / Granzin, J. / Stoldt, M. / Henklein, P. / Ernst, O.P. / Heck, M. / Willbold, D. / Koenig, B. W.
Contributing Institute:	Strukturbiochemie; ISB-3
Published in:	Biochemistry, 48 (2009) S. 10733 -10742
Imprint:	Columbus, Ohio American Chemical Society 2009
Physical Description:	10733 -10742
DOI:	10.1021/bi900544p
PubMed ID:	19835414
Document Type:	Journal Article
Research Program:	Funktion und Dysfunktion des Nervensystems
Series Title:	Biochemistry 48
Subject (ZB):	Arrestin: chemistry Models, Molecular Nuclear Magnetic Resonance, Biomolecular Photochemistry Protein Conformation Rhodopsin: chemistry Arrestin Rhodopsin J
	Publikationsportal JuSER

Please use the identifier: http://dx.doi.org/10.1021/bi900544p in citations.

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.