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. Author manuscript; available in PMC: 2009 Nov 7.
Published in final edited form as: Mol Cell. 2008 Nov 7;32(3):394–405. doi: 10.1016/j.molcel.2008.09.017

Figure 1. Structure and Inhibitor of the Extended Kinase Domain of Bub1.

Figure 1

(A) Domain architecture of human Bub1. TPR, tetratricopeptide repeat; GLEBS, Gle2-binding sequence; KEN, lysine-glutamate-asparagine.

(B) Ribbon drawing of the crystal structure of the extended kinase domain of Bub1. The N-terminal extension is colored yellow. The substrate-binding P+1 loop is shown in green while the rest of the activation segment is in blue. The catalytic loop is shown in red. ATP is shown as sticks. The Mg2+ ion is shown as a gray sphere. The N- and C-termini are indicated. All structure figures were generated with PyMOL (http://pymol.sourceforge.net/).

(C) The ATP-binding site of Bub1. ATP is shown as sticks. The extra pocket is indicated.

(D) The chemical structure of 2OH-BNPP1.

(E) Determination of the IC50 values of 2OH-BNPP1 against Aurora B, p38, Bub1C, and Bub1.