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![[Figure 4]](cb5141fig4mag.jpg)
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Figure 4
AAR2-mediated blocking of a step 2 conformation in PRPF8RH. (a–d) Structure of the AAR2Δloop–PRPF8RH complex (a) and close-up views comparing the AAR2Δloop C-terminal tail (sticks) traversing the PRPF8 RH domain below the protruding β-finger module (surface views) as observed in the AAR2Δloop–PRPF8RH complex (b) or modeled onto the PRPF8RH domain in the step 1 conformation (PDB entry 4jk7; Schellenberg et al., 2013  ) (c) or onto the PRPF8RH domain in the step 2 conformation (PDB entry 4jk7; Schellenberg et al., 2013) (d) by superposition of the RH domains. Yellow sphere, coordinated Mg2+ ion. The AAR2 C-terminus clashes with the PRPF8RH domain in the step 2 conformation. (e–h) SDS–PAGE analyses (left) and UV elution profiles (right) of analytical size-exclusion chromatography runs monitoring the interaction between AAR2 and PRPF8RH (e, g) or PRPF8RH,T1789P (f, h) at 2 mM (e, f) or 40 mM (g, h) magnesium chloride. Lane M, molecular-mass standard (kDa); lane I, input samples. Protein bands are identified on the right. Elution fractions are indicated at the top of the gel and profile in (e); elution volumes are indicated at the bottom of the profile in (h). Icons are explained at the bottom left. Variants are indicated below the respective icons. Peaks labeled with transparent icons represent an excess of the respective protein. |
![[Figure 4]](cb5141fig4.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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