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Figure 4.
The putative phospholipid-binding site. A, Fe65-PTB1 (color
ramps as in Figs. 2 and 3) superposed with the
Dab1-PTB-APP-IP[3] complex (PDB code 1oqn) shown in gray and
black. Residues involved in IP[3] binding and the equivalent
three arginines of Fe65-PTB1 are given. Although helix α2 in
Dab1 is elongated by two turns, Fe65-PTB1 contains a long and
flexible α2/β2 loop. B, electrostatic surface potential of the
Dab1-PTB domain showing the highly positively charged
phospholipid binding crown responsible for IP[3] binding (stick
model). Color scheme is as in Fig. 2. C, Fe65-PTB1 oriented in
the same way with superposed IP[3] taken from the Dab1-PTB
structure.
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