ArticleThe Journal of biological chemistry2009
Three-dimensional structure of CaV3.1: comparison with the cardiac L-type voltage-gated calcium channel monomer architecture.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed.
- Bioelectricity in dental medicine: a narrative review.Biomedical engineering online · 2024Review
- Regulation of Presynaptic Calcium Channels.Advances in neurobiology · 2023Article
- Nanosecond Pulsed Electric Field (nsPEF): Opening the Biotechnological Pandora's Box.International journal of molecular sciences · 2022Review
- Mechanisms and Regulation of Cardiac CaInternational journal of molecular sciences · 2021Review
- Voltage-gated calcium channels: their discovery, function and importance as drug targets.Brain and neuroscience advances · 2018Article
- An Improved Method for Modeling Voltage-Gated Ion Channels at Atomic Accuracy Applied to Human CaCell reports · 2018Article
- Role of individual S4 segments in gating of CaChannels (Austin, Tex.) · 2018Article
- Calmodulin regulates CaThe Journal of biological chemistry · 2017Article
- Negatively charged residues in the first extracellular loop of the L-type CaThe Journal of biological chemistry · 2017Article
- Voltage-gated calcium channels and their auxiliary subunits: physiology and pathophysiology and pharmacology.The Journal of physiology · 2016Review
- The α2δ-1 subunit remodels CaV1.2 voltage sensors and allows Ca2+ influx at physiological membrane potentials.The Journal of general physiology · 2016Article
- Identification of Glycosylation Sites Essential for Surface Expression of the CaVα2δ1 Subunit and Modulation of the Cardiac CaV1.2 Channel Activity.The Journal of biological chemistry · 2016Article
- Genetic disruption of voltage-gated calcium channels in psychiatric and neurological disorders.Progress in neurobiology · 2015Review
- The Physiology, Pathology, and Pharmacology of Voltage-Gated Calcium Channels and Their Future Therapeutic Potential.Pharmacological reviews · 2015Review
- The molecular architecture of dihydropyrindine receptor/L-type Ca2+ channel complex.Scientific reports · 2015Article
- Selectivity filters and cysteine-rich extracellular loops in voltage-gated sodium, calcium, and NALCN channels.Frontiers in physiology · 2015Review
- Functional exofacially tagged N-type calcium channels elucidate the interaction with auxiliary α2δ-1 subunits.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- 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
- Characterization of the molecular architecture of human caveolin-3 and interaction with the skeletal muscle ryanodine receptor.The Journal of biological chemistry · 2012Article
- Calcium channel auxiliary α2δ and β subunits: trafficking and one step beyond.Nature reviews. Neuroscience · 2012Review
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Authors and funding
5 authors.
Funding
Abstract
Calcium entry through voltage-gated calcium channels has widespread cellular effects upon a host of physiological processes including neuronal excitability, muscle excitation-contraction coupling, and secretion. Using single particle analysis methods, we have determined the first three-dimensional structure, at 23 A resolution, for a member of the low voltage-activated voltage-gated calcium channel family, CaV3.1, a T-type channel. CaV3.1 has dimensions of approximately 115x85x95 A, composed of two distinct segments. The cytoplasmic densities form a vestibule below the transmembrane domain with the C terminus, unambiguously identified by the presence of a His tag being approximately 65 A long and curling around the base of the structure. The cytoplasmic assembly has a large exposed surface area that may serve as a signaling hub with the C terminus acting as a "fishing rod" to bind regulatory proteins. We have also determined a three-dimensional structure, at a resolution of 25 A, for the monomeric form of the cardiac L-type voltage-gated calcium (high voltage-activated) channel with accessory proteins beta and alpha2delta bound to the ion channel polypeptide CaV1.2. Comparison with the skeletal muscle isoform finds a good match particularly with respect to the conformation, size, and shape of the domain identified as that formed by alpha2. Furthermore, modeling of the CaV3.1 structure (analogous to CaV1.2 at these resolutions) into the heteromeric L-type voltage-gated calcium channel complex volume reveals multiple interaction sites for beta-CaV1.2 binding and for the first time identifies the size and organization of the alpha2delta polypeptides.
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