IndraLab

Statements

Potassium channel toxin gamma-KTx 1.1 binds KCNH2. 22 / 22
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"Specifically, we have shown that incomplete block is due to the forward and backward rate constants for the final rearrangements, which must be made for the toxin-channel encounter complex to form the[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
17369411
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"Consequently, at 37°C, ∼60% of encounters are unproductive compared to ∼30% at 22°C.This suggests that the temperature-dependent changes in the CnErg1 binding to hERG could be explained by decreased s[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Of the three PSSs, two were found to be involved in the binding of ErgTx1 to hERG channel."
23103547
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"The functional importance of Q18A and M35A provides a new clue for understanding the interaction between ErgTx1 and hERG1."
23103547
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"Supported by these analyses, a rational interaction between ErgTx1 and hERG1 is established ( Fig. 4 B), which might improve the previous model proposed only based on evolutionary trace analysis [3,11[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
23103547
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"Cysteine scanning mutagenesis studies of the S5-P and P-S6 linker regions of the channel demonstrated that the residues that contribute most to the tight interaction of the complex hERG1-ErgTx1 are, i[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
20600425
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"However, in the binding of ErgTx1 to hERG1 the electrostatic interactions should not be the main force for toxin binding."
20600425
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"However, a detailed analysis of the kinetics of CnErg1 binding to hERG revealed that association rates are not diffusion-limited."
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"Theoretically this device permits solution changes within 10 ms; however, our own tests with altering external K + concentrations indicated that the time constant for solution change was 24 ± 2.5 ms ([MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"The plot of [T] k +1 against [T] (shown in Fig. 7, B and C ) is clearly nonlinear, indicating that binding of CnErg1 to hERG is not diffusion-limited."
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"There are, however, a number of questions about how CnErg1 binds to hERG that need to be answered before we can use this toxin to gain insights into the structure of the unique outer pore domain of hE[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"However, CnErg1 binding to hERG is not sensitive to changes in [K + ] and is relatively insensitive to changes in ionic strength of the extracellular solutions (16) ."
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"These atypical features of CnErg1 binding to hERG are very similar to those for BeKm-1 binding to hERG (41) ."
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"The experimental data presented in this study disproves both of these hypotheses with respect to CnErg1 binding to hERG."
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"Thus, despite its simplicity, this kinetic scheme provides an accurate model of CnErg1 binding to hERG channels.The K d for CnErg1 block of hERG channels increased approximately ninefold between 22°C [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
17369411
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"A key observation we have made in this study is that binding of CnErg1 to hERG is not diffusion-limited ( Figs."
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"Therefore, to fully understand CnErg1 binding to hERG we need to understand not just the blocked toxin-channel complex but also the toxin-channel encounter complex.To derive unique global solutions fo[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"It should be noted that the binding of CnErg1 (see Supplementary Material ) and the related toxin BeKm1 (45) to hERG varies according to the voltage protocol used to elicit current during toxin bindin[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"The mechanistic insight gained from this study is, therefore, generally applicable to CnErg1 binding to hERG, and not limited to the specific voltage protocol used.It is also important to highlight th[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"The binding of Ergtoxin to HERG channels, however, is not influenced by the extracellular [K +] and does not involve strong electrostatic interactions [12]."
12650941
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"It is therefore likely that hydrophobic interactions will play a more important role in Ergtoxin binding to HERG than is the case for other scorpion toxins binding to their respective ion-channel rece[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
12650941
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"Electrostatic interactions are much less important for ErgTx1 binding to HERG channels than for AgTx2 binding to Shake r channels, although these interactions can not be ruled out completely."
12967767