Crystallographic insights into sodium-channel modulation by the β4 subunit
Copyright policy )Crystallographic insights into sodium-channel modulation by the β4 subunit
Significance Voltage-gated sodium (Na v ) channels are members of a large complex that plays a crucial role in rapid electrical signaling throughout the human body. As prominent members of this complex, β-subunits modify Na v channel function and cause debilitating disorders when mutated. Collectively, the functional and crystallographic results reported in this work uncover intricate interactions of these elements within the Na v -channel signaling complex and establish a key role for β-subunits in shaping Na v 1.2 pharmacology. An important concept emerging from our results is that β-subunits provide exciting opportunities for designing new therapeutic strategies to correct their abnormal behaviors.
- Vrije Universiteit Brussel Belgium
- Johns Hopkins University School of Medicine United States
- Johns Hopkins University United States
- Johns Hopkins Medicine United States
- University of British Columbia Canada
Epilepsy, NAV1.2 Voltage-Gated Sodium Channel, Cysteine/chemistry, Voltage-Gated Sodium Channel beta-4 Subunit, Voltage-Gated Sodium Channel beta-1 Subunit/chemistry, Voltage-Gated Sodium Channel beta-4 Subunit/chemistry, Mutation, Missense, Voltage-Gated Sodium Channel beta-1 Subunit, Structure-activity relationship, Crystallography, X-Ray, Epilepsy/genetics, Protein Structure, Secondary, Protein Structure, Tertiary, Structure-Activity Relationship, Xenopus laevis, NAV1.2 Voltage-Gated Sodium Channel/chemistry, Amino Acid Substitution, Animals, Humans, Cysteine
Epilepsy, NAV1.2 Voltage-Gated Sodium Channel, Cysteine/chemistry, Voltage-Gated Sodium Channel beta-4 Subunit, Voltage-Gated Sodium Channel beta-1 Subunit/chemistry, Voltage-Gated Sodium Channel beta-4 Subunit/chemistry, Mutation, Missense, Voltage-Gated Sodium Channel beta-1 Subunit, Structure-activity relationship, Crystallography, X-Ray, Epilepsy/genetics, Protein Structure, Secondary, Protein Structure, Tertiary, Structure-Activity Relationship, Xenopus laevis, NAV1.2 Voltage-Gated Sodium Channel/chemistry, Amino Acid Substitution, Animals, Humans, Cysteine
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