|
Figure 2.
Figure 2: Architecture of the VchIntIA–VCR[bs] synapse.
Figure 2 : Architecture of the VchIntIA–VCRbs synapse.
Unfortunately we are unable to provide accessible
alternative text for this. If you require assistance to access
this image, or to obtain a text description, please contact
npg@nature.com-
a, N-terminal view of the complex. Four VchIntIA molecules
bind two antiparallel VCR[bs] duplexes to form the active
synapse. The extrahelical base T12" (red) is stabilized by cis
interactions and is involved with DNA site recognition (Fig. 4a,
b). The extrahelical base G20" (blue) is buried in subunits that
are bound to the other VCR[bs] duplex forming a set of trans
interactions (Fig. 4c, d). The non-symmetric interfaces between
VchIntIA molecules yield a two-fold symmetric synapse. b,
Orthogonal view with respect to a. The C-terminal helices (N)
bury one face in a hydrophobic pocket of the adjacent subunit in
a cyclic manner (N[A] arrow
B, N[B] arrow
C, and so on).
|