%0 Journal Article
%A Granzin, J.
%A Cousin, A.
%A Weirauch, M.
%A Schlesinger, R.
%A Büldt, G.
%A Batra-Safferling, R.
%T Crystal structure of p44, a constitutively active splice variant of visual arrestin
%J Journal of molecular biology
%V 416
%N 5
%@ 0022-2836
%C Amsterdam [u.a.]
%I Elsevier
%M PreJuSER-111980
%P 611 - 618
%D 2012
%Z 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.
%X 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.
%K Animals
%K Arrestin: chemistry
%K Arrestin: genetics
%K Arrestin: metabolism
%K Cattle
%K Crystallography, X-Ray: methods
%K Genetic Variation
%K Light Signal Transduction
%K Models, Molecular
%K Phosphorylation
%K Protein Binding
%K Protein Structure, Tertiary: genetics
%K RNA Splicing
%K Rhodopsin: metabolism
%K Static Electricity
%K Arrestin (NLM Chemicals)
%K Rhodopsin (NLM Chemicals)
%K J (WoSType)
%F PUB:(DE-HGF)16
%9 Journal Article
%$ pmid:22306737
%U <Go to ISI:>//WOS:000301682800001
%R 10.1016/j.jmb.2012.01.028
%U https://juser.fz-juelich.de/record/111980