IndraLab

Statements

Potassium channel toxin gamma-KTx 2.1 binds KCNH2. 11 / 11
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"To study the mechanism of BeKm-1 action, we characterize BeKm-1 and HERG interaction in terms of its sensitivity to changes in the extracellular or intracellular ionic composition and to changes in me[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
12719233
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"Therefore, these aspects are where we begin to characterize BeKm-1 and HERG interaction and to deduce the mechanism of toxin action.We examine the effects of 1-1000 nM BeKm-1 on the HERG current ampli[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
12719233
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"It is therefore possible that the binding of BeKm-1 to hERG occurs via the same mechanism as that for CnErg1."
17369411
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"The models were further restrained based on mutant cycle analysis of BeKm-1 and hERG interactions."
17293393
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"It is important to point out that although such a strong state dependence of BeKm-1 and hERG interactions appears similar to that of " gating modifying toxins " that bind to the S3-S4 linkers of targe[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
17293393
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"This result is consistent with our hypothesis that the structure of the S5-P linker is highly dynamic, and can be easily perturbed by mutations, toxin binding, or conformational changes in other parts[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
17293393
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"Here, we used molecular dynamics and ensemble docking, guided by previous double-mutant cycle analysis data, to obtain an in silico model of the hERG-BeKm-1 complex."
38563123
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"Starting from the hERG and BeKm-1 structures, a considerably reasonable BeKm-1 and hERG complex structure was then screened out and identified by protein protein docking, molecular dynamics (MD) simulations, and calculation of relative binding free energies."
17269718
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"BeKm-1 binds to hERG's outer vestibule to suppress ion conduction through the pore."
18687312
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"Mutant cycle analysis earlier published by Tseng et al. [27] , provides mechanistic insights into the unique features of BeKm-1/hERG interaction."
18687312
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"These atypical features of CnErg1 binding to hERG are very similar to those for BeKm-1 binding to hERG (41) ."
17369411