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- W2075517963 abstract "In excitable cells, the initiation of an action potential results from the opening of voltage-gated sodium channels. In humans, mutations in different sodium channel isoforms have been shown to have causal relationships with neurological and cardiovascular diseases, and they therefore represent key targets for development of pharmaceutical drugs. Sodium channels are also present in some prokaryotes, where they appear to function in homeostasis, motility, and chemotaxis. All sodium channels undergo a series of conformational changes associated with their open, closed and inactivated functional states.We have determined the crystal structure of the open conformation of the NavMs bacterial sodium channel pore (McCusker et al, 2012). It contrasts with the structure (Payandeh et al, 2011) of a closely-related bacterial channel, NavAb, which has a closed pore conformation. The differences, which in the open form produce an internal cavity accessible to the cytoplasmic surface, result from a bend/rotation about a central residue in the C-terminal transmembrane segment. The open activation gate is of sufficient diameter to allow passage of hydrated sodium ions. Comparisons between the forms suggest a mechanism of channel opening and closing which differs both from that of potassium channels, and from existing models for sodium channel opening/closing. Comparisons of the selectivity filters and fenestrations further suggest features important both for activity and for the design of new state-specific ligands/drugs." @default.
- W2075517963 created "2016-06-24" @default.
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- W2075517963 date "2013-01-01" @default.
- W2075517963 modified "2023-09-29" @default.
- W2075517963 title "The Open Conformation of a Voltage-Gated Sodium Channel Reveals the Transmembrane Pathway and Gating Mechanism" @default.
- W2075517963 doi "https://doi.org/10.1016/j.bpj.2012.11.063" @default.
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