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Literature DB >> 29043505

Structural and Functional Analysis of Sodium Channels Viewed from an Evolutionary Perspective.

Tamer M Gamal El-Din¹, Michael J Lenaeus², William A Catterall².

Abstract

Voltage-gated sodium channels initiate and propagate action potentials in excitable cells. They respond to membrane depolarization through opening, followed by fast inactivation that terminates the sodium current. This ON-OFF behavior of voltage-gated sodium channels underlays the coding of information and its transmission from one location in the nervous system to another. In this review, we explore and compare structural and functional data from prokaryotic and eukaryotic channels to infer the effects of evolution on sodium channel structure and function.

Entities: Chemical

Keywords: Activation mechanisms; Bacterial sodium channels; Eukaryotic sodium channels; Evolution of sodium channels; Gating mechanisms; Inactivation mechanisms; Selectivity of sodium channels

Mesh：

Substances：

Year: 2018 PMID： 29043505 DOI： 10.1007/164_2017_61

Source DB: PubMed Journal: Handb Exp Pharmacol ISSN： 0171-2004

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Cited

7 in total

1. Structural Basis for High-Affinity Trapping of the Na_V1.7 Channel in Its Resting State by Tarantula Toxin.

Authors: Goragot Wisedchaisri; Lige Tonggu; Tamer M Gamal El-Din; Eedann McCord; Ning Zheng; William A Catterall
Journal: Mol Cell Date: 2020-11-23 Impact factor: 17.970

2. Molecular dissection of multiphase inactivation of the bacterial sodium channel Na_VAb.

Authors: Tamer M Gamal El-Din; Michael J Lenaeus; Karthik Ramanadane; Ning Zheng; William A Catterall
Journal: J Gen Physiol Date: 2018-12-03 Impact factor: 4.086

3. Myasthenic congenital myopathy from recessive mutations at a single residue in Na_V1.4.

Authors: Nathaniel Elia; Johanna Palmio; Marisol Sampedro Castañeda; Perry B Shieh; Marbella Quinonez; Tiina Suominen; Michael G Hanna; Roope Männikkö; Bjarne Udd; Stephen C Cannon
Journal: Neurology Date: 2019-03-01 Impact factor: 11.800

4. New Insights into the Type II Toxins from the Sea Anemone Heteractis crispa.

Authors: Rimma S Kalina; Steve Peigneur; Elena A Zelepuga; Pavel S Dmitrenok; Aleksandra N Kvetkina; Natalia Y Kim; Elena V Leychenko; Jan Tytgat; Emma P Kozlovskaya; Margarita M Monastyrnaya; Irina N Gladkikh
Journal: Toxins (Basel) Date: 2020-01-10 Impact factor: 4.546

Structural and Functional Analysis of Sodium Channels Viewed from an Evolutionary Perspective.

1. Structural Basis for High-Affinity Trapping of the Na_V1.7 Channel in Its Resting State by Tarantula Toxin.

2. Molecular dissection of multiphase inactivation of the bacterial sodium channel Na_VAb.

3. Myasthenic congenital myopathy from recessive mutations at a single residue in Na_V1.4.

4. New Insights into the Type II Toxins from the Sea Anemone Heteractis crispa.

5. Structural basis for voltage-sensor trapping of the cardiac sodium channel by a deathstalker scorpion toxin.

Review 6. Fenestropathy of Voltage-Gated Sodium Channels.

Review 7. Druggability of Voltage-Gated Sodium Channels-Exploring Old and New Drug Receptor Sites.

Structural and Functional Analysis of Sodium Channels Viewed from an Evolutionary Perspective.

1. Structural Basis for High-Affinity Trapping of the NaV1.7 Channel in Its Resting State by Tarantula Toxin.

2. Molecular dissection of multiphase inactivation of the bacterial sodium channel NaVAb.

3. Myasthenic congenital myopathy from recessive mutations at a single residue in NaV1.4.

4. New Insights into the Type II Toxins from the Sea Anemone Heteractis crispa.

5. Structural basis for voltage-sensor trapping of the cardiac sodium channel by a deathstalker scorpion toxin.

Review 6. Fenestropathy of Voltage-Gated Sodium Channels.

Review 7. Druggability of Voltage-Gated Sodium Channels-Exploring Old and New Drug Receptor Sites.

1. Structural Basis for High-Affinity Trapping of the Na_V1.7 Channel in Its Resting State by Tarantula Toxin.

2. Molecular dissection of multiphase inactivation of the bacterial sodium channel Na_VAb.

3. Myasthenic congenital myopathy from recessive mutations at a single residue in Na_V1.4.