IndraLab

Statements

RPS6 binds KCNQ1. 4 / 4
| 4
sparser
"Previous studies have shown that the transmembrane region of KCNE1 adopts an α-helical structure [ xref ], and interacts with the KCNQ1 pore-lining S6 domain to modulate channel activity [ xref ]."
20196769
sparser
"The contrasting effects of MinK and MiRP2 on KCNQ1 activation are striking given that only subtle differences have been found in their interaction with the KCNQ1 S6 pore-lining domain ( xref , xref ; xref )."
17227916
sparser
"Structural modeling indicated that the S338F mutation specifically alters the interaction between the S6 domain of one KCNQ1 subunit and the S4-S5 linker of another, inhibiting voltage-induced movement synergistically with KCNE1 binding."
23291057
sparser
"Cysteine cross-linking indicates that the proximal KCNE1 COOH terminus is in interaction with the KCNQ1 S4/S5 linker and S6 gate, key structures of the gating machinery (Lvov et al., xref )."
22529812