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| Hauptseite > Publikationsdatenbank > N-terminal and C-terminal Domains of Arrestin Both Contribute in Binding to Rhodopsin (dagger) > print |
| Hauptseite > Publikationsdatenbank > N-terminal and C-terminal Domains of Arrestin Both Contribute in Binding to Rhodopsin (dagger) > print |
| 001 | 57375 | ||
| 005 | 20200402210142.0 | ||
| 024 | 7 | _ | |2 pmid |a pmid:17132044 |
| 024 | 7 | _ | |2 DOI |a 10.1562/2006-08-25-RA-1014 |
| 024 | 7 | _ | |2 WOS |a WOS:000245658000025 |
| 037 | _ | _ | |a PreJuSER-57375 |
| 041 | _ | _ | |a eng |
| 082 | _ | _ | |a 570 |
| 084 | _ | _ | |2 WoS |a Biochemistry & Molecular Biology |
| 084 | _ | _ | |2 WoS |a Biophysics |
| 100 | 1 | _ | |a Skegro, D. |b 0 |0 P:(DE-HGF)0 |
| 245 | _ | _ | |a N-terminal and C-terminal Domains of Arrestin Both Contribute in Binding to Rhodopsin (dagger) |
| 260 | _ | _ | |a Malden, Mass. |b Wiley-Blackwell |c 2007 |
| 300 | _ | _ | |a 385 - 393 |
| 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 Photochemistry and Photobiology |x 0031-8655 |0 15281 |v 83 |
| 500 | _ | _ | |a Record converted from VDB: 12.11.2012 |
| 520 | _ | _ | |a Visual arrestin terminates the signal amplification cascade in photoreceptor cells by blocking the interaction of light activated phosphorylated rhodopsin with the G-protein transducin. Although crystal structures of arrestin and rhodopsin are available, it is still unknown how the complex of the two proteins is formed. To investigate the interaction sites of arrestin with rhodopsin various surface regions of recombinant arrestin were sterically blocked by different numbers of fluorophores (Alexa 633). The binding was recorded by time-resolved light scattering. To accomplish site-specific shielding of protein regions, in a first step all three wild-type cysteines were replaced by alanines. Nevertheless, regarding the magnitude and specificity of rhodopsin binding, the protein is still fully active. In a second step, new cysteines were introduced at selected sites to allow covalent binding of fluorophores. Upon attachment of Alexa 633 to the recombinant cysteines we observed that these bulky labels residing in the concave area of either the N- or the C-terminal domain do not perturb the activity of arrestin. By simultaneously modifying both domains with one Alexa 633 the binding capacity was reduced. The presence of two Alexa 633 molecules in each domain prevented binding of rhodopsin to arrestin. This observation indicates that both concave sites participate in binding. |
| 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 Arrestin: chemistry |
| 650 | _ | 2 | |2 MeSH |a Arrestin: genetics |
| 650 | _ | 2 | |2 MeSH |a Arrestin: metabolism |
| 650 | _ | 2 | |2 MeSH |a Base Sequence |
| 650 | _ | 2 | |2 MeSH |a Binding Sites |
| 650 | _ | 2 | |2 MeSH |a Cattle |
| 650 | _ | 2 | |2 MeSH |a Cysteine: chemistry |
| 650 | _ | 2 | |2 MeSH |a DNA Primers: genetics |
| 650 | _ | 2 | |2 MeSH |a Fluorescent Dyes |
| 650 | _ | 2 | |2 MeSH |a Models, Molecular |
| 650 | _ | 2 | |2 MeSH |a Mutagenesis, Site-Directed |
| 650 | _ | 2 | |2 MeSH |a Photochemistry |
| 650 | _ | 2 | |2 MeSH |a Protein Binding |
| 650 | _ | 2 | |2 MeSH |a Protein Structure, Tertiary |
| 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 Rhodopsin: metabolism |
| 650 | _ | 2 | |2 MeSH |a Signal Transduction |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Arrestin |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a DNA Primers |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Fluorescent Dyes |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Recombinant Proteins |
| 650 | _ | 7 | |0 52-90-4 |2 NLM Chemicals |a Cysteine |
| 650 | _ | 7 | |0 9009-81-8 |2 NLM Chemicals |a Rhodopsin |
| 650 | _ | 7 | |a J |2 WoSType |
| 700 | 1 | _ | |a Pulvermuller, A. |b 1 |0 P:(DE-HGF)0 |
| 700 | 1 | _ | |a Krafft, B. |b 2 |0 P:(DE-HGF)0 |
| 700 | 1 | _ | |a Granzin, J. |b 3 |u FZJ |0 P:(DE-Juel1)131965 |
| 700 | 1 | _ | |a Hofmann, K. P. |b 4 |0 P:(DE-HGF)0 |
| 700 | 1 | _ | |a Büldt, G. |b 5 |u FZJ |0 P:(DE-Juel1)131957 |
| 700 | 1 | _ | |a Schlesinger, R. |b 6 |u FZJ |0 P:(DE-Juel1)VDB1421 |
| 773 | _ | _ | |a 10.1562/2006-08-25-RA-1014 |g Vol. 83, p. 385 - 393 |p 385 - 393 |q 83<385 - 393 |0 PERI:(DE-600)2048860-9 |t Photochemistry and photobiology |v 83 |y 2007 |x 0031-8655 |
| 856 | 7 | _ | |u http://dx.doi.org/10.1562/2006-08-25-RA-1014 |
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| 914 | 1 | _ | |y 2007 |
| 915 | _ | _ | |0 StatID:(DE-HGF)0010 |a JCR/ISI refereed |
| 920 | 1 | _ | |k INB-2 |l Molekulare Biophysik |d 31.12.2008 |g INB |0 I:(DE-Juel1)VDB805 |x 0 |
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| 980 | _ | _ | |a UNRESTRICTED |
| 980 | _ | _ | |a I:(DE-Juel1)ICS-6-20110106 |
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| 981 | _ | _ | |a I:(DE-Juel1)ICS-6-20110106 |
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