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 (FBP21 326-376), which are sufficient to fully form the interaction with the C-terminal Sec63 unit of Brr2 (Brr2 C-Sec63), adopt a random coil conformation in their unbound state.