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Figure 2.
Figure 2. A, Portion of a CNS all omit map covering the
vicinity of the phosphate ion linking the segment of the
polypeptide at the immediate N terminus of helix-1 with the
middle section of helix-3. (Liganding to Glu146 is not shown for
clarity, see the text.) B, Schematic representation of the sheep
PrP molecule. The helices, labelled H1-H3, are shown in blue,
and the short segments of anti-parallel b-sheet are shown in
red. C, Schematic representation of the helix-swapped dimer
structure of the human prion protein.[6.] The bottom half of the
dimer is in the same orientation as the sheep PrP shown in B and
similarly coloured, but with H3 in light blue. The dyad-related
monomer is at the top and its b-strands are coloured in green.
The helices for the dyad-related molecule are distinguished by a
prime. The exchange of H3 and H3' is accompanied by the
formation of an additional segment of anti-parallel b-sheet,
coloured in red and green (Figure drawn with Spock).
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