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. 2014 Jul 25;592(Pt 20):4465–4480. doi: 10.1113/jphysiol.2014.277483

Figure 1. hERG1 concatenated tetramers and location of mutated residues characterized in this study.

Figure 1

A, positioning of WT and mutant hERG1 subunits in seven different concatenated tetramers. The restriction enzymes used to link KCNH2 cDNAs are also indicated. B, location of residues in a hERG1 subunit that were mutated in this study, including Thr618 and Ser620 in the pore helix, Gly628 in the selectivity filter, Ser631 outside the selectivity filter, and Met645 in the S6 segment. Also shown is Asn629 that can interact with Ser620. Homology model of a single S5-S6 region of hERG1 was based on the KcsA channel structure (PDB ID: 1BL8) and prepared using YASARA (Krieger et al. 2009).