ArticleProtein science : a publication of the Protein Society2006
Solution structure of the N-terminal A domain of the human voltage-gated Ca2+channel beta4a subunit.
Article in Protein science : a publication of the Protein Society, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 20 citations in OpenAlex.
- β subunits of voltage-gated calcium channels in cardiovascular diseases.Frontiers in cardiovascular medicine · 2023Review
- Article
- Presynaptic voltage-gated calcium channels in the auditory brainstem.Molecular and cellular neurosciences · 2021Review
- Structure and function of the β subunit of voltage-gated Ca²⁺ channels.Biochimica et biophysica acta · 2013Review
- Three-dimensional localization of the α and β subunits and of the II-III loop in the skeletal muscle L-type Ca2+ channel.The Journal of biological chemistry · 2012Article
- The Ca2+ channel beta4c subunit interacts with heterochromatin protein 1 via a PXVXL binding motif.The Journal of biological chemistry · 2011Article
- The ß subunit of voltage-gated Ca2+ channels.Physiological reviews · 2010Review
- Genomic organization, expression, and phylogenetic analysis of Ca2+ channel beta4 genes in 13 vertebrate species.Physiological genomics · 2008Article
- The calcium channel beta4a subunit: a scaffolding protein between voltage-gated calcium channel and presynaptic vesicle-release machinery?The Journal of neuroscience : the official journal of the Society for Neuroscience · 2006Article
- Alternative splicing of the voltage-gated Ca2+ channel beta4 subunit creates a uniquely folded N-terminal protein binding domain with cell-specific expression in the cerebellar cortex.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2006Article
- Progress in the structural understanding of voltage-gated calcium channel (CaV) function and modulation.Channels (Austin, Tex.)Review
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Authors and funding
4 authors at 2 institutions in 1 country.
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Abstract
Ca2+ channel beta subunits regulate trafficking and gating (opening and closing) of voltage-dependent Ca2+ channel alpha1 subunits. Based on primary sequence comparisons, they are thought to be modular structures composed of five domains (A-E) that are related to the large family of membrane associated guanylate-kinase (MAGUK) proteins. The crystal structures of the beta subunit core, B-D, domains have recently been reported; however, very little is known about the structures of the A and E domains. The N-terminal A domain is a hypervariable region that differs among the four subtypes of Ca2+ channel beta subunits (beta1-beta4). Furthermore, this domain undergoes alternative splicing to create multiple N-terminal structures within a given gene class that have distinct effects on gating. We have solved the solution structure of the A domain of the human beta4a subunit, a splice variant that we have shown previously to have alpha1 subunit subtype-specific effects on Ca2+ channel trafficking and gating.
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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.