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Inhibitory Kappa B kinase α (IKKα) inhibitors that recapitulate their selectivity in cells against isoform-related biomarkers

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Figure

Figure 1. Sequence alignment for the kinase domains of IKKα and IKKβ (4KIK_chainB) showing 61% of identical residues (colored in turquoise), afurther 14% similar residues (polar for polar, hydrophobic for hydrophobic; in light blue), and 25% nonsimilar residues (white).
Figure 3. Superimposition of IKKthe binding pocket of IKK(Asn28, Gln48, and Pro52) engaged in dianalogue as a stick model) between the two isoforms
Table 1. Biochemical Inhibitory Data for the N4-Substituted 2-Amino-5-cyanopyrrolo[2,3-d]pyrimidinesa
Table 1. continued
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