ArticleBiophysical journal2004
Structural effects of an LQT-3 mutation on heart Na+ channel gating.
Article in Biophysical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 24 citations in OpenAlex.
- Functional cross-talk between phosphorylation and disease-causing mutations in the cardiac sodium channel NaProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Mexiletine Treatment for Neonatal LQT3 Syndrome: Case Report and Literature Review.Frontiers in pediatrics · 2021Article
- Detection of NaBiophysical journal · 2019Article
- Distribution of cardiac sodium channels in clusters potentiates ephaptic interactions in the intercalated disc.The Journal of physiology · 2018Article
- Calmodulin limits pathogenic Na+ channel persistent current.The Journal of general physiology · 2017Article
- Cardiac Na Channels: Structure to Function.Current topics in membranes · 2016Article
- Voltage-gated sodium channel-associated proteins and alternative mechanisms of inactivation and block.Cellular and molecular life sciences : CMLS · 2012Review
- Mechanistic links between Na+ channel (SCN5A) mutations and impaired cardiac pacemaking in sick sinus syndrome.Circulation research · 2010Article
- Solution structure of the NaV1.2 C-terminal EF-hand domain.The Journal of biological chemistry · 2009Article
- Distinct functional defect of three novel Brugada syndrome related cardiac sodium channel mutations.Journal of biomedical science · 2009Article
- Using computational modeling to predict arrhythmogenesis and antiarrhythmic therapy.Drug discovery today. Disease models · 2009Article
- Mutation of sodium channel SCN3A in a patient with cryptogenic pediatric partial epilepsy.Neuroscience letters · 2008Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Computational methods that predict three-dimensional structures from amino acid sequences have become increasingly accurate and have provided insights into structure-function relationships for proteins in the absence of structural data. However, the accuracy of computational structural models requires experimental approaches for validation. Here we report direct testing of the predictions of a previously reported structural model of the C-terminus of the human heart Na(+) channel. We focused on understanding the structural basis for the unique effects of an inherited C-terminal mutation (Y1795C), associated with long QT syndrome variant 3 (LQT-3), that has pronounced effects on Na(+) channel inactivation. Here we provide evidence that this mutation, in which a cysteine replaces a tyrosine at position 1795 (Y1795C), enables the formation of disulfide bonds with a partner cysteine in the channel. Using the predictions of the model, we identify the cysteine and show that three-dimensional information contained in the sequence for the channel protein is necessary to understand the structural basis for some of the effects of the mutation. The experimental evidence supports the accuracy of the predicted structural model of the human heart Na(+) channel C-terminal domain and provides insight into a structural basis for some of the mutation-induced altered channel function underlying the disease phenotype.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.