Figure 1.
Fig. 1. The sequence of the protein construct used in the
present work and its relation to the nominal PH domain and to
the G[ ]-binding
region of ARK1. At the
top is the nominal length PH domain section; below is the domain
demonstrated previously (50) to be sufficient and optimal for G[
]binding,
below which is the construct used here, which has the same G[
]binding.
The lowercase "gshm" residues are from the GST construct, and^
are not further referred to. At the bottom, the complete
sequence^ of h ARK1 PH
domain, and the similar h ARK2 are
compared, with the secondary structural elements of h ARK1
superimposed in color. The more flexible region of the
C-terminal -helix is
shown in light blue.
The above figure is reprinted
by permission from the ASBMB:
J Biol Chem
(1998,
273,
2835-2843)
copyright 1998.
]-binding
region of 
ARK1. At the
top is the nominal length PH domain section; below is the domain
demonstrated previously (50) to be sufficient and optimal for G[
-helix is
shown in light blue.