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.
The above figure is reprinted
by permission from Macmillan Publishers Ltd:
Nature
(2001,
411,
215-219)
copyright 2001.
-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.