|
Figure 4.
FIGURE 4. TREX1 structure reveals PPII helix. a, the
non-repetitive proline-rich region within TREX1 forms a PPII.
The PPII helix, made up of residues 54–62, has a tight,
3-sided, left-handed secondary structure. PPII helices often
function as interaction motifs with other proteins containing
SH3, WW, or EVH1 domains. b, location of PPII helices (shown in
red) within the TREX1 dimer. The positioning on opposite outer
edges of the same face of the dimer might play a key role in
TREX1 protein interactions by allowing for simultaneous binding
of multiple interaction domains to the dimer.
|
