Comparison of the B-Myb, STAT1, E1A and p53 transactivation domain binding sites on p300/CBP TAZ2.

<p>Panel A shows a contact surface view of CBP TAZ2 (top) with the location of the B-Myb TAD binding site on p300 TAZ2 highlighted as described in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0052906#pone-0052906-g005" target="_blank">figure 5</a>. For comparison, the structures of STAT1 TAD-CBP TAZ2 (row 2; PDB code 2KA6), E1A CR1-CBP TAZ2 (row 3; PDB code 2KJE) and p53 TAD1-p300 TAZ2 (row 4 PDB code 2K8F) are shown in the same orientation <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0052906#pone.0052906-Wojciak1" target="_blank">[56]</a>, <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0052906#pone.0052906-Ferreon1" target="_blank">[61]</a>, <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0052906#pone.0052906-Feng1" target="_blank">[64]</a>, with the TAZ2 domain shown as a contact surface and the STAT1 TAD, E1A CR1 and p53 TAD1 as a ribbon representation of their backbone conformation. Only the well defined residues of STAT1 (721–750), E1A (53–83) and p53 (9–31) that contact TAZ2 are shown in the figure. The views in panels B and C are rotated about the y axis by 90° and −90° compared to panel A. Panel D shows the structure of STAT1 TAD-CBP TAZ2, in the same orientation shown in panel A, with the TAZ2 domain shown as a contact surface and STAT1 TAD as a ribbon representation of the domain. TAZ2 residues are coloured on the basis of residue type, with basic amino acids in blue (Arg, Lys and His), acidic in red (Asp and Glu), polar in orange (Ser, Thr, Asn and Gln), cysteine in green and hydrophobic in white (Trp, Phe, Tyr, Ala, Val, Ile, Leu, Met, Pro and Gly).