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. Author manuscript; available in PMC: 2019 Aug 4.
Published in final edited form as: Neuroscience. 2018 May 29;384:152–164. doi: 10.1016/j.neuroscience.2018.05.031

Figure 2: Identification of mutation in human KCNJ6.

Figure 2:

(A) Sequencing of patient and parent DNA revealed a mutation in KCNJ6. Cartoon shows position of L171R mutation in GIRK2 ion channel (M1, M2: transmembrane domains; P: pore). (B) 3D structural model of human GIRK2 obtained by homology modeling from mouse GIRK2 channel (PDB: 3SYO). The mutation L171R allows Arg171 to potentially form H-bonds with Glu148 in the adjacent subunit. This electrostatic interaction could produce a more stable structure and impair conformational movements, i.e., opening/closing of the channel, or alter ion selectivity. (C) A detail of the 3D structural model of human KCNJ6 shows the network of interactions (H-bonds) that stabilize the conformation of the outer part (the selectivity filter) of the KCNJ6 channel.