TY  - JOUR
AU  - Granzin, J.
AU  - Cousin, A.
AU  - Weirauch, M.
AU  - Schlesinger, R.
AU  - Büldt, G.
AU  - Batra-Safferling, R.
TI  - Crystal structure of p44, a constitutively active splice variant of visual arrestin
JO  - Journal of molecular biology
VL  - 416
IS  - 5
SN  - 0022-2836
CY  - Amsterdam [u.a.]
PB  - Elsevier
M1  - PreJuSER-111980
SP  - 611 - 618
PY  - 2012
N1  - We are grateful to the beamline scientists at the European Synchrotron Radiation Facility (Grenoble, France) for providing assistance with the use of beamline ID14-4. We thank Oliver H. Weiergraber for comments on the manuscript, Bianca Krafft for generating the p44 clone in S. cerevisiae, and Dieter Willbold and the Russian Group ONEXIM (GB) for generous support.
AB  - Visual arrestin specifically binds to photoactivated and phosphorylated rhodopsin and inactivates phototransduction. In contrast, the p44 splice variant can terminate phototransduction by binding to nonphosphorylated light-activated rhodopsin. Here we report the crystal structure of bovine p44 at a resolution of 1.85 Å. Compared to native arrestin, the p44 structure reveals significant differences in regions crucial for receptor binding, namely flexible loop V-VI and polar core regions. Additionally, electrostatic potential is remarkably positive on the N-domain and the C-domain. The p44 structure represents an active conformation that serves as a model to explain the 'constitutive activity' found in arrestin variants.
KW  - Animals
KW  - Arrestin: chemistry
KW  - Arrestin: genetics
KW  - Arrestin: metabolism
KW  - Cattle
KW  - Crystallography, X-Ray: methods
KW  - Genetic Variation
KW  - Light Signal Transduction
KW  - Models, Molecular
KW  - Phosphorylation
KW  - Protein Binding
KW  - Protein Structure, Tertiary: genetics
KW  - RNA Splicing
KW  - Rhodopsin: metabolism
KW  - Static Electricity
KW  - Arrestin (NLM Chemicals)
KW  - Rhodopsin (NLM Chemicals)
KW  - J (WoSType)
LB  - PUB:(DE-HGF)16
C6  - pmid:22306737
UR  - <Go to ISI:>//WOS:000301682800001
DO  - DOI:10.1016/j.jmb.2012.01.028
UR  - https://juser.fz-juelich.de/record/111980
ER  -