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- W1977453075 abstract "Several homotetrameric ion channels have been crystallized in either the open or closed state. Here we used Monte Carlo-energy minimizations and the program ZMM, which takes advantage of channel symmetry, to simulate activation/deactivation of the pore-forming domains of four channels and estimate their state-dependent energetics. Deactivation of the open-Kv1.2 x-ray structure by a counter-clockwise torque (intracellular view) applied to four S5 N-ends yielded a conformation with S5/S6 alpha-carbons RMS-deviating by 1.8 A from the closed-channel model (Pathak et al., 2007). The data that cadmium binds to the closed Shaker with engineered cysteines in S6s (del Camino et al., 2005) is rationalized in our model with two cadmium ions neutralizing the four ionized cysteines (Bruhova and Zhorov, 2005). Reactivation of our deactivated-Kv1.2 model by the clockwise torque yielded a conformation that RMS-deviates from the open-Kv1.2 structure by 1.4 A. Using the same approach we deactivated and reactivated the pore-domain of KvAP (truncated to match the KcsA-sequence length) and arrived at models with RMSDs of 2.0 and 1.9 A from the KcsA and KvAP x-ray structures, respectively. Activation and deactivation of pH-gated KcsA with centrifugal and centripetal forces, respectively, applied to M2 C-ends (Tikhonov and Zhorov, 2004) yielded conformations that RMS-deviate from the x-ray structures of MthK and KcsA by < 2.0 A. Using the same forces, we activated and deactivated the cyclic-nucleotide gated NaK channel (truncated to match the open-NaK sequence length) and arrived at models with RMSDs ≤ 1.5 A from the closed and open x-ray structures, respectively. In our models, the pore domains of the voltage- and ligand-gated channels are most stable in the open and closed states, respectively, suggesting an intrinsic instability of the pore domains in non-crystallized states. Supported by CIHR and NSERC." @default.
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- W1977453075 date "2010-01-01" @default.
- W1977453075 modified "2023-09-29" @default.
- W1977453075 title "In-Silico Activation and Deactivation of the Pore Domains of Voltage- and Ligand-Gated Ion Channels" @default.
- W1977453075 doi "https://doi.org/10.1016/j.bpj.2009.12.2824" @default.
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