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Figure 3.
Figure 3 Actin-binding extensions of CapZ. (A) The regions
crucial for actin binding [residues 259-C-terminus(  )
and 266-C-terminus(  )],
the segment which exhibits actin-binding ability [residues
253-C-terminus( )]
and the regions that are not required for high-affinity actin
binding [residues N-terminus-115( )
and N-terminus-86( )]
are mapped in red, orange and gray, respectively, on the CapZ
structure based on the previous deletion mutant experiments (Hug
et al., 1992; Casella and Torres, 1994; Sizonenko et al., 1996).
The two conserved arginine residues, Arg259( )
and Arg244( ),
are indicated with ball-and-stick models. (B) Surface
representations of the C-terminal extension (residues 246 -271,
the sole variant region between the isoforms) of two isoforms of
,
1
(the present structure) and 2
(a homology model). The left two panels show the hydrophobic
sides of the helices, and the right two panels show the
hydrophilic sides. Hydrophobic, acidic and basic residues are
colored in yellow, red and blue, respectively. Possible
actin-binding sites are highlighted with red circles. (C)
Surface representations of helix 6 (residues 270 -276) of the
subunit.
The color coding is the same as in (B).
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