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. Author manuscript; available in PMC: 2015 Apr 8.
Published in final edited form as: Structure. 2014 Feb 20;22(4):602–611. doi: 10.1016/j.str.2014.01.008

Figure 5. Mapping NO-induced conformational changes to models of catalytic domain activation.

Figure 5

Catalytic domain exchange rate differences induced by NO were mapped to models of the inactive, “open” conformation and active “closed” conformation. Exchange rate differences are color-coded as in Figure 3; here, α1 and β1 subunits are distinguished as gray and tan, respectively. The open conformation is represented by the structure of the human sGC catalytic domain (PDB: 3UVJ) with GTP docked. The closed conformation is a model based on the structure of a putatively active adenylate cyclase (PDB: 1AZS). Active site aspartate residues, α1 Asp-485 and α1 Asp-529, are highlighted (yellow) in the inset.