Figure 3.
Figure 3: Structure of the Rac -Arfaptin complex. a, Rac
-Arfaptin complex shown in ribbons representation, with Arfaptin
in the same orientation as shown in Fig. 1b, bottom. Helices of
the Rac are red, -strands
are green and the nucleotide is in yellow ball-and-stick
representation. One monomer of the Arfaptin dimer is shown in
blue, the other in pink. b, Arfaptin -Rac interface shown as an
'open book' representation. The C positions
of residues that interact are indicated by white spheres.
Residue type and number are shown in black type with interacting
residues from the other protein indicated in red
(hydrogen-bonding interactions) or green (non-polar/van der
Waals interactions). Asterisk denotes His 57 from Arfaptin
molecule 'B' of the dimer (blue); all other Arfaptin residues
are contributed from molecule 'A' (yellow). The two 'switch'
regions of Rac are highlighted in red.
-strands
are green and the nucleotide is in yellow ball-and-stick
representation. One monomer of the Arfaptin dimer is shown in
blue, the other in pink. b, Arfaptin -Rac interface shown as an
'open book' representation. The C 
positions
of residues that interact are indicated by white spheres.
Residue type and number are shown in black type with interacting
residues from the other protein indicated in red
(hydrogen-bonding interactions) or green (non-polar/van der
Waals interactions). Asterisk denotes His 57 from Arfaptin
molecule 'B' of the dimer (blue); all other Arfaptin residues
are contributed from molecule 'A' (yellow). The two 'switch'
regions of Rac are highlighted in red.