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![[Figure 1]](cb5141fig1mag.jpg)
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Figure 1
(a) Crystal structure of the human AAR2Δloop–PRPF8RH complex. Colour scheme for this and the following figures: AAR2Δloop, orange; PRPF8RH, light blue; dashed orange lines indicate a flexible loop (labeled Ser3) in AAR2 connecting its two domains, which is replaced by three serine residues in AAR2Δloop (Santos et al., 2015  ), and another smaller flexible loop between residues 313 and 321 (labeled flexible loop). The N- and C-termini as well as the β-finger module of PRPF8RH are labeled. (b) Superposition of the RH domains of human PRPF8 and yeast Prp8p in complex with human AAR2Δloop and yeast Aar2p/PRPF8JM (PDB entry 4i43; Galej et al., 2013), respectively, to illustrate the human AAR2 in a larger PRPF8 context. Colour scheme for this and the following figures: Aar2p, maroon; Prp8pRH, dark blue; Prp8pJM, cyan. (c) Comparison of the human AAR2Δloop–PRPF8RH complex and the yeast Aar2pΔloop–Prp8pRH–Prp8pJM complex (PDB entry 4ilg; Weber et al., 2013) by superposition of the RH domains. Dashed maroon line, flexible linker preceding the C-terminal tail of Aar2p (Weber et al., 2013). (d, e) Close-up views of interface regions I of the yeast Aar2pΔloop–Prp8pRH–Prp8pJM complex (d) and the human AAR2Δloop–PRPF8RH complex (e). (f, g) Close-up views of interface regions II of the yeast Aar2pΔloop–Prp8pRH–Prp8pJM complex (f) and the human AAR2Δloop–PRPF8RH complex (g). In (d–f) and the following figures interacting residues are shown as sticks colored by atom type, with carbon colored as the respective protein, nitrogen in blue, oxygen in red and sulfur in yellow; green spheres are water molecules, dashed black lines represent hydrogen bonds or salt bridges and rotation symbols represent orientations relative to (a). |
![[Figure 1]](cb5141fig1.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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