Figure 1.
Figure 1. Structure of the APP N-terminal domain. a, A ribbon
diagram indicating the location of secondary structure. Sheet A
is colored blue, sheet B is in orange and sheet C is shown in
brown. The disulfide bridges are shown in ball-and-stick, and
the tip of the -hairpin
loop is indicated. This figure was drawn with MOLSCRIPT^29. b, A
stereo diagram of a C trace
of the structure, shown in the same orientation as in (a), with
every 20^th residue labeled. c, An orthogonal view drawn as a
CPK representation. Basic residues are in blue, acidic residues
in red, polar residues in pink and hydrophobic residues in
green. The locations of key regions are highlighted. This figure
was drawn with GRASP^30. d, Stereo 2F[o] - F[c] electron density
map (blue), calculated using the final model, at 1.8 Å
resolution. The map is contoured at 1 ,
with the final model overlaid upon it. The region shown
corresponds to part of the hydrophobic core of the protein.
The above figure is reprinted
by permission from Macmillan Publishers Ltd:
Nat Struct Biol
(1999,
6,
327-331)
copyright 1999.
-hairpin
loop is indicated. This figure was drawn with MOLSCRIPT^29. b, A
stereo diagram of a C 
trace
of the structure, shown in the same orientation as in (a), with
every 20^th residue labeled. c, An orthogonal view drawn as a
CPK representation. Basic residues are in blue, acidic residues
in red, polar residues in pink and hydrophobic residues in
green. The locations of key regions are highlighted. This figure
was drawn with GRASP^30. d, Stereo 2F[o] - F[c] electron density
map (blue), calculated using the final model, at 1.8 Å
resolution. The map is contoured at 1 
,
with the final model overlaid upon it. The region shown
corresponds to part of the hydrophobic core of the protein.