Figure 3.
Fig. 3. Structure of the F71N, F82Q, and F92N p18^INK4c
mutants in comparison to the native structure of p18^INK4c
protein. a, superposition of the mutant, F71N (in green) and the
native protein (in gray) along with the simulated annealing omit
map around the site of mutation contoured at 1.5 . The
yellow sphere represents a water molecule. b, detailed
interactions made in the F71N p18^INK4c mutant are shown in
green with CPK coloring, while the structure of the native
protein, which lacks these new interactions are shown in gray.
The mutation results in a new hydrogen-bonding interaction with
arginine 79, and a water (shown in yellow)-mediated hydrogen
bond with aspartate 100. Glycines are shown as green or gray
spheres. c, same as a except that the F82Q mutant is shown. d,
detailed interactions made in the F82Q p18^INK4c mutant are
shown in green with CPK coloring, while the structure of the
native protein, which lacks these, new interactions are shown in
gray. The mutation results in new hydrogen bonding interaction
with the backbone NH of glycine 48 and a water (shown in
yellow)-mediated hydrogen bond with arginine 117. Glycines are
shown as green or gray spheres. e, same as a except that the
F92N mutant is shown. f, detailed interactions made in the F92N
p18^INK4c mutant are shown in green with CPK coloring, while the
structure of the native protein, which lacks these, new
interactions are shown in gray. The mutation results in a new
water-mediated hydrogen bond with arginine 54. Glycines are
shown as green or gray spheres. Molscript objects for the
electron density was created using CONSCRIPT, and the figures
were prepared with the programs MOLSCRIPT (37) and RASTER3D (38).
. The
yellow sphere represents a water molecule. b, detailed
interactions made in the F71N p18^INK4c mutant are shown in
green with CPK coloring, while the structure of the native
protein, which lacks these new interactions are shown in gray.
The mutation results in a new hydrogen-bonding interaction with
arginine 79, and a water (shown in yellow)-mediated hydrogen
bond with aspartate 100. Glycines are shown as green or gray
spheres. c, same as a except that the F82Q mutant is shown. d,
detailed interactions made in the F82Q p18^INK4c mutant are
shown in green with CPK coloring, while the structure of the
native protein, which lacks these, new interactions are shown in
gray. The mutation results in new hydrogen bonding interaction
with the backbone NH of glycine 48 and a water (shown in
yellow)-mediated hydrogen bond with arginine 117. Glycines are
shown as green or gray spheres. e, same as a except that the
F92N mutant is shown. f, detailed interactions made in the F92N
p18^INK4c mutant are shown in green with CPK coloring, while the
structure of the native protein, which lacks these, new
interactions are shown in gray. The mutation results in a new
water-mediated hydrogen bond with arginine 54. Glycines are
shown as green or gray spheres. Molscript objects for the
electron density was created using CONSCRIPT, and the figures
were prepared with the programs MOLSCRIPT (37) and RASTER3D (38).