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Figure 3.
Fig. 3. Phosphoprotein-binding surface of KI-FHA (a, b, and
c) and of FHA2 of RAD53 (d). (a) The class-specific residues at
trace level 9 are blue. (Fig. 6 summarizes the alignment of
class consensus residues at trace level 9.) The residues
identical among KAPP of maize, rice, and Arabidopsis are yellow
in a.(b) KI-FHA residues with amide NMR peaks most shifted by
saturating amounts of the pThr peptide from BAK1 (2 mM
peptide:0.5 mM KI-FHA); i.e., with   [HN] > 0.16 ppm are
red. Those residues with 0.16 ppm > [HN] > 0.06 ppm are
pink. Surface properties of KI-FHA (c) and RAD53 FHA2 (d) are
yellow for hydrophobic, blue for positively charged, and red for
negatively charged residues.
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