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Laboratory of Molecular Biophysics
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| Figure 1. (A) The monomeric PfPK5 fold. The
N-terminal domain (residues 1-82) is coloured white and the C-terminal domain
(residues 83-288) gold. The PfPK5 N- and C-termini are labelled. The
glycine-rich loop (residues 10-19), the C-helix (residues 39-56) and the activation
loop (residues 143-170 from the conserved DFG to APE motifs) are coloured
magenta, red and cyan respectively. (B) Overlay of the structures of monomeric
PfPK5Thr198Ala and CDK2 in the vicinity of the activation loop. CDK2
has been superimposed, coloured pale green. The CDK2 activation loop forms
a b-hairpin that turns across the end of the glycine-loop, while the activation
loop of PfPK5Thr198Ala adopts an extended structure as it stretches away
from aL12 into a short a-helix of 2.5 turns. |
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