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RSS FeedsFBP21`s C-terminal domain remains dynamic when wrapped around the c-Sec63 unit of Brr2 helicase (Biophysical Journal)

 
 

29 november 2018 12:00:08

 
FBP21`s C-terminal domain remains dynamic when wrapped around the c-Sec63 unit of Brr2 helicase (Biophysical Journal)
 




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 FBP21 (FBP21326-376), which are sufficient to fully form the interaction with the C-terminal Sec63 unit of Brr2 (Brr2C-Sec63), adopt a random coil conformation in their unbound state. Upon interaction with Brr2C-Sec63, 42 residues of FBP21326-376 cover the large binding site on Brr2C-Sec63 in an extended conformation.


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26 viewsCategory: Biophysics
 
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