Hauptseite > Publikationsdatenbank > Helix Formation in Arrestin Accompanies Recognition of Photoactivated Rhodopsin > print

001     7146
005     20200402205724.0
024 7 _ |2 pmid
|a pmid:19835414
024 7 _ |2 DOI
|a 10.1021/bi900544p
024 7 _ |2 WOS
|a WOS:000271459100009
037 _ _ |a PreJuSER-7146
041 _ _ |a eng
082 _ _ |a 570
084 _ _ |2 WoS
|a Biochemistry & Molecular Biology
100 1 _ |0 P:(DE-Juel1)VDB89238
|a Feuerstein, S.E.
|b 0
|u FZJ
245 _ _ |a Helix Formation in Arrestin Accompanies Recognition of Photoactivated Rhodopsin
260 _ _ |a Columbus, Ohio
|b American Chemical Society
|c 2009
300 _ _ |a 10733 -10742
336 7 _ |a Journal Article
|0 PUB:(DE-HGF)16
|2 PUB:(DE-HGF)
336 7 _ |a Output Types/Journal article
|2 DataCite
336 7 _ |a Journal Article
|0 0
|2 EndNote
336 7 _ |a ARTICLE
|2 BibTeX
336 7 _ |a JOURNAL_ARTICLE
|2 ORCID
336 7 _ |a article
|2 DRIVER
440 _ 0 |0 798
|a Biochemistry
|v 48
|x 0006-2960
|y 45
500 _ _ |a 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).
520 _ _ |a 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.
536 _ _ |0 G:(DE-Juel1)FUEK409
|2 G:(DE-HGF)
|a Funktion und Dysfunktion des Nervensystems
|c P33
|x 0
588 _ _ |a Dataset connected to Web of Science, Pubmed
650 _ 2 |2 MeSH
|a Arrestin: chemistry
650 _ 2 |2 MeSH
|a Models, Molecular
650 _ 2 |2 MeSH
|a Nuclear Magnetic Resonance, Biomolecular
650 _ 2 |2 MeSH
|a Photochemistry
650 _ 2 |2 MeSH
|a Protein Conformation
650 _ 2 |2 MeSH
|a Rhodopsin: chemistry
650 _ 7 |0 0
|2 NLM Chemicals
|a Arrestin
650 _ 7 |0 9009-81-8
|2 NLM Chemicals
|a Rhodopsin
650 _ 7 |2 WoSType
|a J
700 1 _ |0 P:(DE-HGF)0
|a Pulvermüller, A.
|b 1
700 1 _ |0 P:(DE-Juel1)VDB57647
|a Hartmann, R.
|b 2
|u FZJ
700 1 _ |0 P:(DE-Juel1)131965
|a Granzin, J.
|b 3
|u FZJ
700 1 _ |0 P:(DE-Juel1)VDB21601
|a Stoldt, M.
|b 4
|u FZJ
700 1 _ |0 P:(DE-HGF)0
|a Henklein, P.
|b 5
700 1 _ |0 P:(DE-HGF)0
|a Ernst, O.P.
|b 6
700 1 _ |0 P:(DE-HGF)0
|a Heck, M.
|b 7
700 1 _ |0 P:(DE-Juel1)132029
|a Willbold, D.
|b 8
|u FZJ
700 1 _ |0 P:(DE-Juel1)132009
|a Koenig, B. W.
|b 9
|u FZJ
773 _ _ |0 PERI:(DE-600)1472258-6
|a 10.1021/bi900544p
|g Vol. 48, p. 10733 -10742
|p 10733 -10742
|q 48<10733 -10742
|t Biochemistry
|v 48
|x 0006-2960
|y 2009
856 7 _ |u http://dx.doi.org/10.1021/bi900544p
909 C O |o oai:juser.fz-juelich.de:7146
|p VDB
913 1 _ |0 G:(DE-Juel1)FUEK409
|a DE-HGF
|b Gesundheit
|k P33
|l Funktion und Dysfunktion des Nervensystems
|v Funktion und Dysfunktion des Nervensystems
|x 0
914 1 _ |y 2010
915 _ _ |0 StatID:(DE-HGF)0010
|a JCR/ISI refereed
920 1 _ |0 I:(DE-Juel1)VDB942
|d 31.12.2010
|g ISB
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|l Strukturbiochemie
|x 0
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981 _ _ |a I:(DE-Juel1)IBI-7-20200312
981 _ _ |a I:(DE-Juel1)ICS-6-20110106

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