|
Figure 5.
Fig. 5. Intermolecular interfaces in KCTD5 assemblies. (a)
Potential surfaces of individual KCTD subunit N- and C-modules.
Indicated in red are acidic Asp83, Asp93, Asp95, Asp116, Glu124,
Glu165–Glu167, Glu196, Asp197, Glu182, and Glu208; basic
residues Arg107, Lys110, and Lys115 are indicated in blue.
Gly51, Leu56, Thr57, Thr61, Leu91, Gly100, Asn114, and Gln183
are noted in gray. (b) Secondary structural elements at the
interface of adjacent subunits in the N-module viewed from the
center of the assembly. α-Helices and β-strands are depicted
as cylinders and arrows, respectively. The L1–L4 segments of
the BTB fold are shown in colors as per Fig. 2. Inset presents
an expanded view of the boxed area. Residues that form
interfaces are shown in ball-and-stick in yellow (subunit 1) and
gray (subunit 2). H-bonds (2.6–3.4 Å) are indicated with
dotted lines. Asp116 (subunit 1) and Lys115 (subunit 2) interact
via main-chain atoms, and their side chains are omitted for
clarity. H-bond pairs and distances are noted in further detail
in Fig. S2a. (c) Secondary structural elements at the interface
of adjacent subunits in the C-module viewed from the center of
the assembly as in (b). Inset presents an expanded view of the
boxed area as in (b). H-bond pairs and distances are noted in
further detail in Fig. S2b.
|
