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. 2014 Dec 10;290(4):2431–2443. doi: 10.1074/jbc.M114.616490

FIGURE 3.

FIGURE 3.

The Phe box of BubR1 binds to human Cdc20, but not to human Cdh1. A and B, binding between the indicated GST-BubR1 fragments and in vitro translated 35S-labeled full-length human Cdc20 (A) or Cdh1 (B). The relative binding intensities are indicated below each lane. C, cartoon drawing of the superimposed structures of Saccharomyces cerevisiae (Sc) Cdh1-Acm1 (gray) and human (Hs) Cdc20-BubR1-KEN1 (magenta). The KEN, D, and Phe boxes from Acm1 are colored yellow, with their side chains shown as sticks. D, a close-up view of the Phe box-binding site, with HsCdc20 residues corresponding to the Phe box-binding residues of ScCdh1 shown as magenta sticks. The amino acid types of the corresponding HsCdh1 residues are listed in parentheses. E, binding between GST-BubR1526–546 and in vitro translated 35S-labeled full-length human Cdc20 WT or mutants. The relative binding intensities are indicated below each lane.