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. Author manuscript; available in PMC: 2018 Apr 3.
Published in final edited form as: Trends Cell Biol. 2015 Nov 23;26(3):190–201. doi: 10.1016/j.tcb.2015.10.013

Figure 2. Crystal structure of the human α1β2γ1 heterotrimer in complex with β-cyclodextrin, staurosporine, and AMP, with Thr172 phosphorylated.

Figure 2

Atomic coordinates are from the PDB file 4RER [8]. The model was rendered in PyMOL v1.7.4.2 with the majority of the polypeptide in “cartoon” view and the α-linker in “sphere” view. The domains referred to in the text are color coded and labeled. The kinase inhibitor staurosporine in the active site, and the side chain of phospho-Thr172, are in “sphere” view, and β-cyclodextrin in the glycogen-binding site of the β-CBM in “stick” view, all with C atoms in green, O red, and N blue (H omitted). The curved dotted line in the center shows the approximate boundary between the “catalytic module” (containing the α-KD and β-CBM) and the “nucleotide-binding module” (containing the γ subunit and the C-terminal domains of α and β); the α-AID and α-linker form one of the flexible connectors linking these two modules. Note how the α-RIM2 section of the α-linker (in magenta) contacts site 3 of the γ subunit with its bound AMP.