Home > Publications database > Crystal structure of p44, a constitutively active splice variant of visual arrestin > print

001     111980
005     20240610120407.0
024 7 _ |2 pmid
|a pmid:22306737
024 7 _ |2 DOI
|a 10.1016/j.jmb.2012.01.028
024 7 _ |2 WOS
|a WOS:000301682800001
037 _ _ |a PreJuSER-111980
041 _ _ |a eng
082 _ _ |a 570
084 _ _ |2 WoS
|a Biochemistry & Molecular Biology
100 1 _ |a Granzin, J.
|b 0
|u FZJ
|0 P:(DE-Juel1)131965
245 _ _ |a Crystal structure of p44, a constitutively active splice variant of visual arrestin
260 _ _ |a Amsterdam [u.a.]
|b Elsevier
|c 2012
300 _ _ |a 611 - 618
336 7 _ |a Journal Article
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440 _ 0 |a Journal of Molecular Biology
|x 0022-2836
|0 3552
|y 5
|v 416
500 _ _ |a 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.
520 _ _ |a 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.
536 _ _ |a BioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung
|c P45
|2 G:(DE-HGF)
|0 G:(DE-Juel1)FUEK505
|x 0
536 _ _ |a Funktion und Dysfunktion des Nervensystems
|c P33
|0 G:(DE-Juel1)FUEK409
|x 1
588 _ _ |a Dataset connected to Web of Science, Pubmed
650 _ 2 |2 MeSH
|a Animals
650 _ 2 |2 MeSH
|a Arrestin: chemistry
650 _ 2 |2 MeSH
|a Arrestin: genetics
650 _ 2 |2 MeSH
|a Arrestin: metabolism
650 _ 2 |2 MeSH
|a Cattle
650 _ 2 |2 MeSH
|a Crystallography, X-Ray: methods
650 _ 2 |2 MeSH
|a Genetic Variation
650 _ 2 |2 MeSH
|a Light Signal Transduction
650 _ 2 |2 MeSH
|a Models, Molecular
650 _ 2 |2 MeSH
|a Phosphorylation
650 _ 2 |2 MeSH
|a Protein Binding
650 _ 2 |2 MeSH
|a Protein Structure, Tertiary: genetics
650 _ 2 |2 MeSH
|a RNA Splicing
650 _ 2 |2 MeSH
|a Rhodopsin: metabolism
650 _ 2 |2 MeSH
|a Static Electricity
650 _ 7 |0 0
|2 NLM Chemicals
|a Arrestin
650 _ 7 |0 9009-81-8
|2 NLM Chemicals
|a Rhodopsin
650 _ 7 |a J
|2 WoSType
653 2 0 |2 Author
|a arrestin
653 2 0 |2 Author
|a splice variant
653 2 0 |2 Author
|a p44
653 2 0 |2 Author
|a rhodopsin
653 2 0 |2 Author
|a photoreceptor
700 1 _ |a Cousin, A.
|b 1
|u FZJ
|0 P:(DE-Juel1)VDB31224
700 1 _ |a Weirauch, M.
|b 2
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|0 P:(DE-Juel1)VDB104857
700 1 _ |a Schlesinger, R.
|b 3
|0 P:(DE-HGF)0
700 1 _ |a Büldt, G.
|b 4
|u FZJ
|0 P:(DE-Juel1)131957
700 1 _ |a Batra-Safferling, R.
|b 5
|u FZJ
|0 P:(DE-Juel1)VDB58515
773 _ _ |0 PERI:(DE-600)1355192-9
|a 10.1016/j.jmb.2012.01.028
|g Vol. 416, p. 611 - 618
|p 611 - 618
|q 416<611 - 618
|t Journal of molecular biology
|v 416
|x 0022-2836
|y 2012
|n 5
856 7 _ |u http://dx.doi.org/10.1016/j.jmb.2012.01.028
909 C O |o oai:juser.fz-juelich.de:111980
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