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Figure 4.
Figure 4. Mutation of Asn202 in p65 decreases IkBa binding
affinity of both the NF-kB p65 homodimer and p50/p65
heterodimer. (a) Mutation of NF-kB p65(191-325) homodimer amino
acid residues Asn202 and Ser203 to the corresponding p50 amino
acid residues Thr258 and Ala259 results in a measurable decrease
in IkBa binding affinity (right half) when compared to the
native p65(191-325) homodimer (left half). (b) Mutation of NF-kB
p65(191-325) homodimer Asn202 to Arg, analogous to a genetically
derived mutation that disrupts binding of the Drosophila
homologues Dorsal and Cactus, results in a significant loss of
IkBa binding affinity (compare right and left gel halves). (c) A
decrease in IkBa binding affinity also accompanies incorporation
of the Asn202 to Arg mutation within the context of the NF-kB
p50(245-376)/p65(191-325) heterodimer (compare left and right
gel halves).
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