Figure 1.
Fig. 1. Design of protein assemblies (24). The proteins in (C)
to (H) are depicted as thick-lined C plots at various
scales with mutated residues as colored spheres. (A) Sketch of
an asymmetric interface between patches a and b, which, in
general, gives rise to an infinite helix (top). A C[2]-symmetric
interface also between patches a and b doubles the numbers of
contacts and forms a globular complex (bottom). Along the same
lines, the reported D[2], D[4], and D[8] oligomers have 4-, 8-,
and 16-fold contacts, respectively (fig. S4). (B) Side-chain
mobility of the C[4]-symmetric Rua, color-coded from 0°
(blue) to 90° (red) angular spread in the torsion angles
[1] and [2]
(24). The C- and N-terminal domains are at the top and bottom,
respectively. (C) Pga-A and -B designed in crystal contact
a-a(25). (D) Pga-C and-D designed in crystal contact f-f (25).
(E) Oas-A and-B planned as a D[2] tetramer at a rotation angle
of 86° around a common molecular twofold axis (vertical).
(F) Oas-C designed as a D[2] tetramer at an alternative rotation
angle of 29°. (G) Designed D[2] tetramer of Uro-A around a
common molecular twofold axis (vertical). The designed contact
is between the NAD^+-binding domains (residues 142 to 343),
which are given in lighter hues. (H) Designed octameric Rua-D
with a head-head contact.
The above figure is reprinted
by permission from the AAAs:
Science
(2008,
319,
206-209)
copyright 2008.
plots at various
scales with mutated residues as colored spheres. (A) Sketch of
an asymmetric interface between patches a and b, which, in
general, gives rise to an infinite helix (top). A C[2]-symmetric
interface also between patches a and b doubles the numbers of
contacts and forms a globular complex (bottom). Along the same
lines, the reported D[2], D[4], and D[8] oligomers have 4-, 8-,
and 16-fold contacts, respectively (fig. S4). (B) Side-chain
mobility of the C[4]-symmetric Rua, color-coded from 0°
(blue) to 90° (red) angular spread in the torsion angles
[1] and