TY  - JOUR
AU  - Feuerstein, S.E.
AU  - Pulvermüller, A.
AU  - Hartmann, R.
AU  - Granzin, J.
AU  - Stoldt, M.
AU  - Henklein, P.
AU  - Ernst, O.P.
AU  - Heck, M.
AU  - Willbold, D.
AU  - Koenig, B. W.
TI  - Helix Formation in Arrestin Accompanies Recognition of Photoactivated Rhodopsin
JO  - Biochemistry
VL  - 48
SN  - 0006-2960
CY  - Columbus, Ohio
PB  - American Chemical Society
M1  - PreJuSER-7146
SP  - 10733  -10742
PY  - 2009
N1  - 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).
AB  - 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.
KW  - Arrestin: chemistry
KW  - Models, Molecular
KW  - Nuclear Magnetic Resonance, Biomolecular
KW  - Photochemistry
KW  - Protein Conformation
KW  - Rhodopsin: chemistry
KW  - Arrestin (NLM Chemicals)
KW  - Rhodopsin (NLM Chemicals)
KW  - J (WoSType)
LB  - PUB:(DE-HGF)16
C6  - pmid:19835414
UR  - <Go to ISI:>//WOS:000271459100009
DO  - DOI:10.1021/bi900544p
UR  - https://juser.fz-juelich.de/record/7146
ER  -