Supplementary Figure 3: BRP-HAT interaction and structural details and interaction interfaces.
From: Structure of the p300 catalytic core and implications for chromatin targeting and HAT regulation
(a), The BRP module binds to the HAT domain. Pull–down experiments with GST–BRP against the HAT domain. Input (I), Wash (W) and Bound (B). (b) Isothermal titration calorimetry–based binding curves with wild–type BRP or a Bromodomain mutant BRP N1132. (c) Stereo view of the RING–HAT interface. (d) Crystal packing in the vicinity of the RING domain. The HAT domain (HAT*) of a crystallographically related molecule packs against the RING domain. (e) There are two p300 molecules in the asymmetric crystallographic unit; they overlay well on each other (rmsd 0.9 Å for 564 Ca residues). Coloring as in Figure 1.
