Home > Publications database > Tuning of a neuronal calcium sensor > print

001     54334
005     20200423204409.0
024 7 _ |a pmid:17015448
|2 pmid
024 7 _ |a 10.1074/jbc.M603700200
|2 DOI
024 7 _ |a WOS:000242477100036
|2 WOS
024 7 _ |a 2128/2657
|2 Handle
024 7 _ |a altmetric:3398294
|2 altmetric
037 _ _ |a PreJuSER-54334
041 _ _ |a eng
082 _ _ |a 570
084 _ _ |2 WoS
|a Biochemistry & Molecular Biology
100 1 _ |a Weiergräber, O. H.
|b 0
|u FZJ
|0 P:(DE-Juel1)131988
245 _ _ |a Tuning of a neuronal calcium sensor
260 _ _ |a Bethesda, Md.
|b Soc.
|c 2006
300 _ _ |a 37594 - 37602
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 |a Journal of Biological Chemistry
|x 0021-9258
|0 3091
|v 281
500 _ _ |a Record converted from VDB: 12.11.2012
520 _ _ |a Recoverin is a Ca(2+)-regulated signal transduction modulator expressed in the vertebrate retina that has been implicated in visual adaptation. An intriguing feature of recoverin is a cluster of charged residues at its C terminus, the functional significance of which is largely unclear. To elucidate the impact of this segment on recoverin structure and function, we have investigated a mutant lacking the C-terminal 12 amino acids. Whereas in myristoylated recoverin the truncation causes an overall decrease in Ca(2+) sensitivity, results for the non-myristoylated mutant indicate that the truncation primarily affects the high affinity EF-hand 3. The three-dimensional structure of the mutant has been determined by x-ray crystallography. In addition to significant changes in average coordinates compared with wild-type recoverin, the structure provides strong indication of increased conformational flexibility, particularly in the C-terminal domain. Based on these observations, we propose a novel role of the C-terminal segment of recoverin as an internal modulator of Ca(2+) sensitivity.
536 _ _ |a Funktion und Dysfunktion des Nervensystems
|c P33
|2 G:(DE-HGF)
|0 G:(DE-Juel1)FUEK409
|x 0
588 _ _ |a Dataset connected to Web of Science, Pubmed
650 _ 2 |2 MeSH
|a Animals
650 _ 2 |2 MeSH
|a Base Sequence
650 _ 2 |2 MeSH
|a Calcium Signaling: physiology
650 _ 2 |2 MeSH
|a Cattle
650 _ 2 |2 MeSH
|a Crystallography, X-Ray
650 _ 2 |2 MeSH
|a DNA Primers: genetics
650 _ 2 |2 MeSH
|a Kinetics
650 _ 2 |2 MeSH
|a Models, Molecular
650 _ 2 |2 MeSH
|a Mutagenesis, Site-Directed
650 _ 2 |2 MeSH
|a Protein Structure, Quaternary
650 _ 2 |2 MeSH
|a Recombinant Proteins: chemistry
650 _ 2 |2 MeSH
|a Recombinant Proteins: genetics
650 _ 2 |2 MeSH
|a Recombinant Proteins: metabolism
650 _ 2 |2 MeSH
|a Recoverin: chemistry
650 _ 2 |2 MeSH
|a Recoverin: genetics
650 _ 2 |2 MeSH
|a Recoverin: metabolism
650 _ 2 |2 MeSH
|a Rod Cell Outer Segment: metabolism
650 _ 2 |2 MeSH
|a Sequence Deletion
650 _ 2 |2 MeSH
|a Surface Plasmon Resonance
650 _ 7 |0 0
|2 NLM Chemicals
|a DNA Primers
650 _ 7 |0 0
|2 NLM Chemicals
|a RCV1 protein, Bos taurus
650 _ 7 |0 0
|2 NLM Chemicals
|a Recombinant Proteins
650 _ 7 |0 135844-11-0
|2 NLM Chemicals
|a Recoverin
650 _ 7 |a J
|2 WoSType
700 1 _ |a Senin, I. I.
|b 1
|0 P:(DE-HGF)0
700 1 _ |a Zernii, E.Y.
|b 2
|0 P:(DE-HGF)0
700 1 _ |a Churumova, V. A.
|b 3
|0 P:(DE-HGF)0
700 1 _ |a Kovaleva, N. A.
|b 4
|0 P:(DE-HGF)0
700 1 _ |a Nazipova, A. A.
|b 5
|0 P:(DE-HGF)0
700 1 _ |a Permyakov, S.E.
|b 6
|0 P:(DE-HGF)0
700 1 _ |a Permyakov, E.A.
|b 7
|0 P:(DE-HGF)0
700 1 _ |a Philippov, P.P.
|b 8
|0 P:(DE-HGF)0
700 1 _ |a Granzin, J.
|b 9
|u FZJ
|0 P:(DE-Juel1)131965
700 1 _ |a Koch, K. W.
|b 10
|u FZJ
|0 P:(DE-Juel1)VDB46877
773 _ _ |a 10.1074/jbc.M603700200
|g Vol. 281, p. 37594 - 37602
|p 37594 - 37602
|q 281<37594 - 37602
|0 PERI:(DE-600)1474604-9
|t The @journal of biological chemistry
|v 281
|y 2006
|x 0021-9258
856 7 _ |u http://dx.doi.org/10.1074/jbc.M603700200
|u http://hdl.handle.net/2128/2657
856 4 _ |u https://juser.fz-juelich.de/record/54334/files/85120.pdf
|y OpenAccess
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