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Figure 1.
Fig. 1. (a) Cartoon of the three-dimensional structure of
the intact bPrP(23-230). Helices are green, -strands are
cyan, segments with nonregular secondary structure within the
C-terminal domain are yellow, and the flexibly disordered "tail"
of residues 23-121 is represented by 108 yellow dots, each of
which represents a residue of the tail (the numeration for hPrP
is used, and the insertions and deletions are placed according
to the alignment in ref. 23). (b) Stereo-view of an all-heavy
atom presentation of the globular domain in bPrP(23-230), with
residues 121-230, in the same orientation as in a. The backbone
is shown as a green spline function through the C^ positions,
hydrophobic side chains are yellow, and polar and charged side
chains are violet. (c and d) Surface views of the globular
domains of bPrP and hPrP, respectively. The orientation of the
molecule is slightly changed relative to a, so that the residue
186 is approximately in the center. The electrostatic surface
potential is indicated in red (negative charge), white
(neutral), and blue (positive charge). The figures were prepared
with the program MOLMOL (42).
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