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Figure 5.
Figure 5. Structural differences in the NLS polypeptides of
NF-kB p65 and p65 Asn202Arg homodimers. (a) Ribbon diagram of
the NF-kB p65(191-304) homodimer. A ball and stick
representation of the Asn202 side-chain indicates its position
near the dimer interface in this protein. (b) Similar ribbon
diagram of NF-kB p65(191-304) bearing the Asn202 to Arg
mutation. The mutant Arg side-chain is depicted as a ball and
stick model. (c) Stereoview of electron density from a 2F[O]
-F[C] difference Fourier map contoured at 2s for the region of
the native p65 NLS polypeptide and a crystallographic
neighboring molecule. (d) The same region in the Asn202 to Arg
mutated p65 homodimer displays broken and disordered electron
density for the NLS polypeptide as well as additional side-chain
electron density at the site of mutation. Note the overall
improved electron density for the ordered region of the mutated
protein, which was determined with higher resolution diffraction
data.
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