Figure 3.
Figure 3. Oligomerization of Rad51. (a) The Rad51 filament
assembles by packing a -strand
from the interdomain linker of one protomer (green) onto the
central sheet of the adjacent monomer (yellow). Interactions
between ATPase domains include a helix (purple) that is
disordered in nonfilament structures of RadA and Rad51. (b) A
peptide from BRCA2 (orange) bound to the human Rad51 ATPase
domain (yellow)
(1n0w).
The peptide mimics the -strand
interaction motif of intact Rad51. The loop following the
disordered helix is purple.
The above figure is reprinted
by permission from Macmillan Publishers Ltd:
Nat Struct Mol Biol
(2004,
11,
791-796)
copyright 2004.
-strand
from the interdomain linker of one protomer (green) onto the
central sheet of the adjacent monomer (yellow). Interactions
between ATPase domains include a helix (purple) that is
disordered in nonfilament structures of RadA and Rad51. (b) A
peptide from BRCA2 (orange) bound to the human Rad51 ATPase
domain (yellow)
(