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![[Figure 3]](wa5070fig3mag.jpg)
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Figure 3
Comparison of the dimeric interactions of SARAH domains based on computational alanine scanning. (a, b, c) Ribbon representations depicting the side chains of residues having dimeric interactions derived from the computational alanine scanning of SARAH dimeric interfaces are shown for the MST1–RASSF5 SARAH heterodimer (a), the MST2 SARAH homodimer (b) and the MST1 SARAH homodimer (c). Residues with ΔΔGbind > 1.0 kcal mol−1 in computational alanine scanning are represented as stick models. Among the residues, Trp369, Ile374 and Glu387 of RASSF5 and Phe437 and Leu440 of MST2 are not seen in the figure and are not labelled for clarity. Residues that have polar interactions in the dimeric interface are shown in green. Red balls represent the water molecules mediating the hydrogen bonds between the two protomers. For the MST1–RASSF5 SARAH heterodimer (a), the light blue ribbon represents the backbone structure of the MST1 SARAH domain and the light pink ribbon represents that of the RASSF5 SARAH domain. (d, e) Ribbon representations with the side chains of the hydrophobic core formed by the N-terminal helix–turn–helix region are shown for the MST1 SARAH homodimer (d) and the MST1–RASFF5 SARAH heterodimer (e). Residues with ΔΔGbind > 1.0 kcal mol−1 in computational alanine scanning are shown as yellow sticks. Red sticks represent the side chains that interact with the aromatic residues in the hydrophobic core. Line models represent residues involved in the inter-protomer hydrogen bonding with smaller values of ΔΔGbind than 1.0 kcal mol−1. |
![[Figure 3]](wa5070fig3.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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