Figure 1.
Figure 1: Sequence comparisons, secondary structures and
residues involved in complex formation. a, Sequence of the
Cdc42-binding domain of the ACK tyrosine kinase, showing the
homology to other CRIB-domain proteins. Residues that are
conserved in WASP and PAK1, but not in ACK, are boxed. The -helix
found in free WASP is indicated by a black line. b, Sequence of
Cdc42 compared with that of Rac1. Residues that are different
where Cdc42 contacts f-ACK are boxed. The residues comprising
switch I and switch II are indicated by black lines. In both a
and b, conserved residues involved in the interaction are
coloured yellow (hydrophobic), light green (asparagine,
glutamine, serine and threonine), red (acidic), magenta
(histidine) and dark blue (basic). Blue arrows and grey
cylinders indicate the positions of -strands
and -helices,
respectively, in the Cdc42/f-ACK structure. This Figure was
produced with Alscript^28.
The above figure is reprinted
by permission from Macmillan Publishers Ltd:
Nature
(1999,
399,
384-388)
copyright 1999.
-helix
found in free WASP is indicated by a black line. b, Sequence of
Cdc42 compared with that of Rac1. Residues that are different
where Cdc42 contacts f-ACK are boxed. The residues comprising
switch I and switch II are indicated by black lines. In both a
and b, conserved residues involved in the interaction are
coloured yellow (hydrophobic), light green (asparagine,
glutamine, serine and threonine), red (acidic), magenta
(histidine) and dark blue (basic). Blue arrows and grey
cylinders indicate the positions of 
-strands
and