Academic Journal
N-terminal and C-terminal Domains of Arrestin Both Contribute in Binding to Rhodopsin (dagger)
| العنوان: | N-terminal and C-terminal Domains of Arrestin Both Contribute in Binding to Rhodopsin (dagger) |
|---|---|
| المؤلفون: | Skegro, D., Pulvermuller, A., Krafft, B., Granzin, J., Hofmann, K. P., Büldt, G., Schlesinger, R. |
| المصدر: | Photochemistry and photobiology 83, 385 - 393 (2007). doi:10.1562/2006-08-25-RA-1014 |
| بيانات النشر: | Wiley-Blackwell |
| سنة النشر: | 2007 |
| المجموعة: | Forschungszentrum Jülich: JuSER (Juelich Shared Electronic Resources) |
| مصطلحات موضوعية: | info:eu-repo/classification/ddc/570, Animals, Arrestin: chemistry, Arrestin: genetics, Arrestin: metabolism, Base Sequence, Binding Sites, Cattle, Cysteine: chemistry, DNA Primers: genetics, Fluorescent Dyes, Models, Molecular, Mutagenesis, Site-Directed, Photochemistry, Protein Binding, Protein Structure, Tertiary, Recombinant Proteins: chemistry, Recombinant Proteins: genetics, Recombinant Proteins: metabolism, Rhodopsin: metabolism, Signal Transduction, Arrestin, DNA Primers, Recombinant Proteins, Cysteine, Rhodopsin |
| جغرافية الموضوع: | DE |
| الوصف: | 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. |
| نوع الوثيقة: | article in journal/newspaper |
| اللغة: | English |
| Relation: | info:eu-repo/semantics/altIdentifier/issn/0031-8655; info:eu-repo/semantics/altIdentifier/pmid/pmid:17132044; info:eu-repo/semantics/altIdentifier/wos/WOS:000245658000025; https://juser.fz-juelich.de/record/57375; https://juser.fz-juelich.de/search?p=id:%22PreJuSER-57375%22 |
| الاتاحة: | https://juser.fz-juelich.de/record/57375 https://juser.fz-juelich.de/search?p=id:%22PreJuSER-57375%22 |
| Rights: | info:eu-repo/semantics/closedAccess |
| رقم الانضمام: | edsbas.E22BF7B8 |
| قاعدة البيانات: | BASE |
| الوصف غير متاح. |