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. Author manuscript; available in PMC: 2013 Apr 4.
Published in final edited form as: Cell Mol Life Sci. 2008 Sep;65(17):2637–2657. doi: 10.1007/s00018-008-8086-2

Figure 7.

Figure 7

Interactions of the CaMKI regulatory domain with the catalytic core. Depicted above is a surface rendering of CaMKI with a ribbon diagram of the regulatory domain lying across the face of the molecule. The ATP-binding lobe of the catalytic core is colored dark gray and the substrate-binding domain is light gray. The regulatory domain, which contains both the autoinhibitory and CaM-binding domains, is black. The structure of the regulatory domain is composed of two regulatory helices (αR1 and αR2) connected by a loop. Regulatory helix αR1 makes contacts with the substrate binding domain, blocking interactions with substrate, and αR2 inhibits ATP binding through interactions with residues in the ATP-binding domain.