|
Figure 3.
(a) Close-up of the region of interaction between the
N-terminal RecA-like domain of DBP5 (in blue) and NUP214 (in
green) in the DBP5  N
C–NUP214
 C
structure. The residues involved in hydrophobic and
electrostatic interactions are highlighted. (b) Protein
precipitations by GST pull-downs with DBP5 and NUP214 mutant
proteins. The pull-down assays were carried out as described in
Figure 2a. The DBP5 D223R, I258A, R259D or R262A mutations of
DBP5 impair its interaction with NUP214. NUP214 V353A shows
reduced binding to DBP5, whereas NUP214 D359R impairs the
interaction.
|
