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FBP21’s C-Terminal Domain Remains Dynamic When Wrapped around the c-Sec63 Unit of Brr2 Helicase

Based on our recent finding that FBP21 regulates human Brr2 helicase activity involved in the activation of the spliceosomal B-complex, we investigated the structural and dynamic contribution of FBP21 to the interaction. By using NMR spectroscopy, we could show that the 50 C-terminal residues of FBP...

Täydet tiedot

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Bibliografiset tiedot
Julkaisussa:Biophys J
Päätekijät: Sticht, Jana, Bertazzon, Miriam, Henning, Lisa M., Licha, Jan R., Abualrous, Esam T., Freund, Christian
Aineistotyyppi: Artigo
Kieli:Inglês
Julkaistu: The Biophysical Society 2019
Aiheet:
Linkit:https://ncbi.nlm.nih.gov/pmc/articles/PMC6372199/
https://ncbi.nlm.nih.gov/pubmed/30558886
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.bpj.2018.11.3123
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