Figure 4.
Fig. 4. The effect of the C terminus on the electrostatic
potential of the h ARK1 PH
domain, and comparison with the PLC PH domain.
Surfaces are contoured at 2 kT/e
(red) and 2 kT/e (blue) (GRASP; Ref. 56) for various lengths of
the C-terminal extension: a, full-length construct, 556-670; b,
residues 556-666; c, residues 556-661; d, residues 556-656; e,
nominal PH domain, residues 556-651. The ARK1 PH
domain constructs in b-d correspond to C-terminal deletion
studies of G[ ]binding
(b and c (50) and d^ (19)). The most C-terminal residues, upon
truncation, are indicated. For comparison, the electrostatic
potential of the PH domain from PLC (Protein
Data Bank entry 1MAI) is shown in f; the arrow indicates a
positively charged area at the opening of the -barrel,
which is involved in the phospholipid binding (8). The molecular
orientations are similar, as indicated by the backbone tube
diagrams.
The above figure is reprinted
by permission from the ASBMB:
J Biol Chem
(1998,
273,
2835-2843)
copyright 1998.
ARK1 PH
domain, and comparison with the PLC 
PH domain.
Surfaces are contoured at 
2 kT/e
(red) and 2 kT/e (blue) (GRASP; Ref. 56) for various lengths of
the C-terminal extension: a, full-length construct, 556-670; b,
residues 556-666; c, residues 556-661; d, residues 556-656; e,
nominal PH domain, residues 556-651. The 
]binding
(b and c (50) and d^ (19)). The most C-terminal residues, upon
truncation, are indicated. For comparison, the electrostatic
potential of the PH domain from PLC