 The large majority of studies into the structural basis for KCNE1 modulation of Kv channels focus on its interaction with KCNQ1 (previously named KvLQT1).Residues in the transmembrane domain of KCNE1 lies close to the selectivity filter of KCNQ1 within heteromeric KCNQ1-KCNE1 channel complexes., The C-terminal domain of KCNE1, specifically from amino acids 73 to 79 is necessary for stimulation of slow delayed potassium rectifier current by SGK1.The interaction of KCNE1 with an alpha helix in the S6 KvLQT1 domain contributes to the higher affinity this channel has for benzodiazepine L7 and chromanol 293B by repositioning amino acid residues to allow for this.