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. Author manuscript; available in PMC: 2011 May 28.
Published in final edited form as: J Mol Biol. 2010 Apr 9;399(1):41–52. doi: 10.1016/j.jmb.2010.03.064

Figure 1. The kinase scaffold of the CTD MSK1.

Figure 1

(A) A schematic diagram of the full length MSK1. MSK1 possesses two distinct protein kinase domains that are sequentially activated by phosphorylation at multiple sites. The serine 360, 376, and 381 residues in the hydrophobic linker region are located within the conserved AGC-kinase sequence. The arrow indicates the sites phosphorylated by CTD MSK1 and MAP kinases. A ribbon diagram (B) and electrostatic surface (C) representation of CTD MSK1 (residues 414-738) are shown. The helices and strands are colored in blue and silver, respectively. The C-terminal extension (i.e, the αK and αL-helices) is shown in red, the AMP-PNP molecule is shown in sticks (pink), and the disordered T-loop is shown as a dotted line.