Figure 2.
FIGURE 2. Overall structure of human Mps1 catalytic domain.
A, ribbon representation of the structure of Mps1 kinase domain.
Characteristic key features important for substrate binding and
catalysis are labeled as follows: glycine loop (orange), C helix,
catalytic loop (cyan), and activation loop with DFG motif (blue)
and p + 1 loop (purple). B, comparison of Mps1 apo-WT (green)
and T686A (brown) with phosphorylated Aurora A (P-ArA, red, PDB
ID 1OL5) and unphosphorylated Aurora A (unP-ArA, gray, PDB ID
1MUO). Displacement of helix C, due to the conformation of the
activation loop in the unphosphorylated structures, results in a
shift of the glutamic acid residue and loss of interaction with
the catalytically important lysine. C, superposition of the p +
1 loop between WT apo-kinase (green) and T686A-SP600125 complex
(gold). The positions of Thr-686 and Ala-686 are indicated.
The above figure is reprinted
by permission from the ASBMB:
J Biol Chem
(2008,
283,
21495-21500)
copyright 2008.
C helix,
catalytic loop (cyan), and activation loop with DFG motif (blue)
and p + 1 loop (purple). B, comparison of Mps1 apo-WT (green)
and T686A (brown) with phosphorylated Aurora A (P-ArA, red, PDB
ID 1OL5) and unphosphorylated Aurora A (unP-ArA, gray, PDB ID
1MUO). Displacement of helix C, due to the conformation of the
activation loop in the unphosphorylated structures, results in a
shift of the glutamic acid residue and loss of interaction with
the catalytically important lysine. C, superposition of the p +
1 loop between WT apo-kinase (green) and T686A-SP600125 complex
(gold). The positions of Thr-686 and Ala-686 are indicated.