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Figure 4.
Figure 4 Comparison of TLP-  with
other -propeller
domains from compartmentalized proteases. (a) Ribbon diagram of
TLP- as
viewed along the sevenfold pseudo-symmetry axis. The nine
aspartate residues forming the negative ring at the entrance to
the channel are highlighted as a ball-and-stick model. (b)
Electrostatic surface representation of TLP- in
top, bottom and cut-open side views. Negative surface charges
are coloured red and positive charges blue. (c) Surface
representation (colour codes: aromatic, green; aliphatic,
yellow; polar, cyan; charged, grey) showing the interior side of
the channel of the superimposed structures of TLP- (I),
POP (II), TRI- 7
(III) and DPP-IV (IV) from the bottom view.
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