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- W1995996060 abstract "Voltage-gated ion channels (VGIC) are proteins that form transmembrane pores in cell membranes. Based on the crystal structure of an open potassium channel (KV) that reveals the bending of a glycine residue in the inner helix that lines the pore (M2 or S6), and the conserved pore sequences in many members of the VGIC superfamily, is thought that the opening mechanism might be quite similar within the family. In fact, this has been demonstrated for a bacterial sodium channel (NaV). However, in LVA calcium channels, the mid-S6 hinge glycine residue is present only in IS6 and IIS6, suggesting a likely different opening mechanism. Here, we explored this possibility in the CaV3.3 member of LVA channels by performing a mutational analysis of the two conserved glycines (Gly385 and Gly814), and a valine (Val1383) in IIIS6 which, according to sequence similarity, corresponds to a hinge glycine in KV and NaV channels. Substitution of Gly814 for proline (G814P) or alanine (G814A), as well as the mutant V1383G, drastically decreased whole-cell current density, with discrete effects on the voltage-dependence of activation. However, the mutant G814P displayed a 10 mV shift in the steady-state inactivation curve to hyperpolarized potentials; the current inactivation kinetics was slowed down by 50%, and the recovery was also more than two-fold slower. The substitution by proline also increased the channel closing time constant by 60%; this effect was also displayed by mutant V1383G, which in addition induced the strongest effect on the inactivation kinetics slowing (≥ 2-fold). Our preliminary results suggest that residues Gly814 and Val1383 are mostly involved in the inactivation gating and, in a lesser degree, stabilizing the open state of CaV3.3. Additional mutations, including double and triple substitutions, are currently under investigation. Supported by CONACYT México J50250Q." @default.
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- W1995996060 date "2011-02-01" @default.
- W1995996060 modified "2023-10-03" @default.
- W1995996060 title "Role of the Putative Glycines Hinge of Cav3.3 Channels" @default.
- W1995996060 doi "https://doi.org/10.1016/j.bpj.2010.12.3302" @default.
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