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Figure 1.
Figure 1. The location of the peptide-binding sites on
phospho-CDK2 -cyclin A3 complex. CDK2 is shown in yellow with
the C (PSTAIRE) helix in red and the activation segment in
magenta. Cyclin A3 is shown in khaki. a, Conventional view of
the CDK2 -cyclin A3 complex, also showing the peptide substrate
(green ball-and-stick diagram) and the recruitment peptide (cyan
ball-and-stick diagram). Note that the structures of the
phospho-CDK2 -cyclin A3 -peptide complexes were determined
separately. b, Dimeric phospho-CDK2 -cyclin A3 complexes. The
phospho-CDK2 -cyclin A3 -peptide complexes in the crystal formed
dimers, with the two complexes related by a non-crystallographic
two-fold axis, in an arrangement similar to that of the
phospho-CDK2 -cyclin A3 crystal (coordinates 1JST)5, which
crystallized in a different space group to the peptide
complexes. The contacts across the dimer interface are between
the  -sheet
region of CDK2 (end of 2
and start of 3)
and the groove between helices in cyclin A3 (helices  3
and 5).
c, Surface representation of the substrate-peptide-binding
pocket of CDK2, showing the site for proline at P+1 and the
proximity of lysine at P+3 to cyclin A3. d, Surface
representation of the recruitment-peptide complex. Diagrams
generated in AESOP (M.E.M.N., unpublished observations).
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