IndraLab

Statements

RPS6 binds KCNH2. 5 / 5
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sparser
"Interestingly, one d-sotalol (0) or l-sotalol(+) molecule was observed to bind deep into the hERG pore, just below the SF region and interact with the canonical drug binding F656 and Y652 hERG residues [ xref – xref ] in the pore lining S6 helices (drug molecule M2 in xref and xref ) for most of 8 μs long MD runs, while another drug molecule was observed to transiently bind below, interacting with F656 and/or Y652 from another domain as well as S660 and other residues at the bottom of S6 helices (M1 in xref and xref )."
34062207
sparser
"Thus, it seems reasonable to propose that lidocaine is also likely to interact with S6 aromatic residues of hERG and our docking data ( xref and S5) support such a conclusion."
24877995
sparser
"Altogether, these observations confirmed that the paradoxical activation effect initially observed when S4-S5 L (0) peptide was co-transfected with WT hERG channel was not due to an interaction of this peptide with the S6 T region of hERG."
28273916
sparser
"Interestingly, for l-sotalol(0) and d-sotalol(+) systems, we observed only transient binding of one or two drug molecules at the bottom of hERG channel pore interacting with S660 and other S6 helix residues there ( xref and xref and xref and xref ) Hence up to two sotalol molecules were able to bind to the hERG pore, in agreement with our electrophysiological data (as described below)."
34062207
sparser
"The direct block was mediated by drug binding to S6 domain of the hERG subunit, while trafficking deficiency was mediated by binding to a different site or a related protein. xref In this study, we used site-directed mutagenesis to test whether Y652A or F656V mutation alter the BBR sensitivity of hERG after long-term treatment."
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