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Figure 2.
Figure 2. Interactions of distinct NLSs with Kapa. The NLS
peptides (shown in colour) nestle between the conserved Trp-Asn
pairs of residues that line the surface of Kapa. Each pair is
provided by a single ARM repeat, shaping the regularly spaced P
and P' specificity pockets at the large and small binding sites,
respectively. The polar and electrostatic interactions between
conserved protein and NLS residues are indicated with dotted
lines. (a) Schematic diagram of the interactions between the
human c-myc NLS peptide (highlighted in blue) and yeast Kapa.
The monopartite NLS binds at the large (functional) and small
sites with mainchain and sidechain interactions. (b) Schematic
diagram of the interactions between the Xenopus nucleoplasmin
NLS peptide (highlighted in pink) and protein residues. The
bipartite NLS binds along the whole surface groove with
mainchain and sidechain interactions at the small site, and with
mainly backbone interactions of the linker and the downstream
cluster.
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