Figure 5.
Figure 5 IQ motif-binding interface of Mlc1p. (A) Compact
conformation of the Mlc1p -IQ2 complex. The view is along the
axis of the -helices
of IQ2 (shown in green). The amino acids of Mlc1p are colored
yellow, except for those amino acids that make direct contacts
with the IQ peptide, which are depicted in red (the same amino
acids are also colored red in Figure 3A). Two views are shown:
on the left side of the figure, the IQ peptide has been moved
out of its binding cleft manually to illustrate better the
binding interface, while the view on the right side corresponds
to the actual position of the IQ peptide in the crystal
structure. (B) Extended structure of Mlc1p -IQ4 (same color
scheme and orientation as A). Note how all of the amino acids of
the N-lobe that interact with IQ2 in the compact structure
become solvent exposed in this complex. The resulting surface
would be available for interactions with a GxxxR-containing
target without a need for the N-lobe to open.
The above figure is reprinted
from an Open Access publication published by Macmillan Publishers Ltd:
EMBO J
(2003,
22,
362-371)
copyright 2003.
-helices
of IQ2 (shown in green). The amino acids of Mlc1p are colored
yellow, except for those amino acids that make direct contacts
with the IQ peptide, which are depicted in red (the same amino
acids are also colored red in Figure 3A). Two views are shown:
on the left side of the figure, the IQ peptide has been moved
out of its binding cleft manually to illustrate better the
binding interface, while the view on the right side corresponds
to the actual position of the IQ peptide in the crystal
structure. (B) Extended structure of Mlc1p -IQ4 (same color
scheme and orientation as A). Note how all of the amino acids of
the N-lobe that interact with IQ2 in the compact structure
become solvent exposed in this complex. The resulting surface
would be available for interactions with a GxxxR-containing
target without a need for the N-lobe to open.