|
Figure 3.
Figure 3 (a) General overview of the complex between trypsin
from F. oxysporum and LMPI-3 from L. migratoria. The trypsin is
represented as a ribbon diagram (coloured grey) and its surface
is shown as half-transparent. Residue Gly173 is coloured red.
The residues Asp189 (specificity pocket) and Ser195 (catalytic
serine) are depicted as sticks and coloured cyan. The inhibitor
LMPI-3 is in ribbon representation and is coloured green. The
disulfide bridges of LMPI-3 are shown in orange. The residue
Arg29 (P1) is depicted as sticks and coloured magenta. The
figure was generated using PyMOL (DeLano, 2002[DeLano, W. L.
(2002). The PyMOL Molecular Graphics System.
http://www.pymol.org .]). (b) Interaction surfaces of F.
oxysporum trypsin and of LMPI-3. The two partners of the complex
are represented as grey molecular surfaces and the amino acids
that are buried upon binding are labelled and are coloured cyan
(trypsin) and magenta (inhibitor). This figure was generated
using PyMOL.
|
