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. 2018 Feb 5;150(2):225–244. doi: 10.1085/jgp.201711898

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© 2018 James and Zagotta

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms/). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 International license, as described at https://creativecommons.org/licenses/by-nc-sa/4.0/).

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Figure 5. — Overview of the five CNBD channel structures. For each channel, the core domains of one subunit are colored as in Fig. 3 (VSD in gray, pore domain in red, C-linker domain in green, and CNBD in blue). Additional domains and/or associated regulatory proteins are colored separately, whereas bound cyclic nucleotides or intrinsic ligand residues are shown as yellow sticks. (A) The rEAG1 (PDB ID: 5K7L) channel, with the N-terminal eag domain shown in orange and one bound Ca²⁺-calmodulin shown in cyan. (B) The hERG1 (PDB ID: 5VA1) channel, with the N-terminal eag domain shown in orange. (C) The hHCN1 channel bound by cAMP (PDB ID: 5U6P), with the N-terminal HCN domain shown in light brown. (D) C. elegans CNG channel (TAX-4, PDB ID: 5H3O) bound by cGMP. (E) Leptospira licerasiae bacterial CNG channel (LliK, PDB ID: 5V4S) in the presence of cAMP.