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Figure 4.
Figure 4: Cul1-Skp1-F boxSkp2 interface and the putative
protein-binding site on other cullins. a, View of the
interface between Cul1 (dark green) and Skp1-F boxSkp2 (blue and
magenta) in an orientation rotated 90° about the vertical axis
of Fig. 1. The residues of Cul1, Skp1, and F-boxSkp2 that are
involved in the interactions are shown in light green, cyan and
pink colours, respectively. Hydrogen bonds are indicated by
white dotted lines. b, Sequence alignments of the orthologues of
Cul2, Cul3 and Cul5 in the regions that correspond to the Skp1-F
boxSkp2 binding site of Cul1. Invariant residues are highlighted
in yellow. Cul4B is not shown because only human and fly
sequences are available. The published Cul4A sequence lacks most
of the first cullin repeat. c, The sequence of Cul3 was mapped
onto the structure of the Cul1 NTD on the basis of sequence
homology, and the resulting model's surface was coloured
according to conservation in Cul3 orthologues. The model surface
shows that the residues identical in Cul3 orthologues (yellow)
cluster on the same surface region as the Skp1-F boxSkp2 binding
site of Cul1 (Fig. 2b). A Cul5 model constructed the same way
shows a similar feature.
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