ArticleProceedings of the National Academy of Sciences of the United States of America1991
Dihydropyridine receptor of L-type Ca2+ channels: identification of binding domains for [3H](+)-PN200-110 and [3H]azidopine within the alpha 1 subunit.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 148 citations in OpenAlex.
- Effects of prototypic calcium channel blockers in methadone-maintained humans responding under a naloxone discrimination procedure.European journal of pharmacology · 2013Trial
- Inhibition of CaV1.4 channels by CaV3 channel antagonists ML218 and Z944.The Journal of general physiology · 2026Article
- The molecular transition that confers voltage dependence to muscle contraction.Nature communications · 2025Article
- Voltage gated sodium and calcium channels: Discovery, structure, function, and Pharmacology.Channels (Austin, Tex.) · 2023Review
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- Genetic disruption of voltage-gated calcium channels in psychiatric and neurological disorders.Progress in neurobiology · 2015Review
- Structural Basis for Pharmacology of Voltage-Gated Sodium and Calcium Channels.Molecular pharmacology · 2015Review
- Calcium Channel CaVα₁ Splice Isoforms - Tissue Specificity and Drug Action.Current molecular pharmacology · 2015Review
- Increased intracellular magnesium attenuates β-adrenergic stimulation of the cardiac Ca(V)1.2 channel.The Journal of general physiology · 2013Article
- Upregulation of the CaV 1.1-ryanodine receptor complex in a rat model of critical illness myopathy.American journal of physiology. Regulatory, integrative and comparative physiology · 2011Article
- Interaction of diltiazem with an intracellularly accessible binding site on Ca(V)1.2.British journal of pharmacology · 2011Article
- Structural model for phenylalkylamine binding to L-type calcium channels.The Journal of biological chemistry · 2009Article
- L-type voltage-dependent calcium channel antagonists impair perirhinal long-term recognition memory and plasticity processes.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2009Article
- Channeling studies in yeast: yeast as a model for channelopathies?Neuromolecular medicine · 2006Review
- Functional architecture of the inner pore of a voltage-gated Ca2+ channel.The Journal of general physiology · 2005Article
- Human cardiac potassium channel DNA polymorphism modulates access to drug-binding site and causes drug resistance.The Journal of clinical investigation · 2005Article
- The L-type calcium channel alpha 1C subunit gene undergoes extensive, uncoordinated alternative splicing.Molecular and cellular biochemistry · 2005Article
- Molecular pharmacology of high voltage-activated calcium channels.Journal of bioenergetics and biomembranes · 2003Review
- Molecular basis of drug interaction with L-type Ca2+ channels.Journal of bioenergetics and biomembranes · 1998Review
- Construction of a high-affinity receptor site for dihydropyridine agonists and antagonists by single amino acid substitutions in a non-L-type Ca2+ channel.Proceedings of the National Academy of Sciences of the United States of America · 1997Article
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3 authors at 1 institution in 1 country.
Funding
Abstract
To identify the binding domain for dihydropyridine Ca2+ antagonists, skeletal muscle Ca2+ channels were photolabeled with [3H](+)-PN200-110 and [3H]azidopine. Regions of alpha 1 photolabeled by these ligands were then identified by antibody mapping of proteolytic fragments. Approximately 50% of the specific labeling by both ligands was incorporated in domain III. [3H]Azidopine labeled peptide Gln-989-Arg-1022, which contains a portion of the connecting loop between transmembrane segments IIIS5 and IIIS6 (IIIS5/S6), and peptide Ala-1023-Lys-1077, which contains IIIS6 itself and some adjacent amino acid residues. In contrast, [3H](+)-PN200-110 labeling occurred almost exclusively in the fragment containing IIIS6. A second site labeled by both ligands was identified in transmembrane segment S6 of domain IV and adjacent residues. In contrast to azidopine, the photoreactive benzofurazane group of (+)-PN200-110 is located in close proximity to the essential dihydropyridine ring. Therefore, the regions photolabeled by [3H](+)-PN200-110 within or adjacent to transmembrane segments IIIS6 and IVS6 must participate in the formation of the dihydropyridine binding site. As IIIS5/S6 is preferentially labeled by [3H]azidopine, it may contribute to drug binding by interaction with the long side chain of some dihydropyridines like azidopine. It is proposed, based on physiological studies, that these three peptide segments interact to form a receptor site accessible from the extracellular surface of the Ca2+ channel.
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