A Molecular Determinant of Nickel Inhibition in Cav3.2 T-type Calcium Channels

Molecular cloning studies have revealed that heterogeneity of T-type Ca2+ currents in native tissues arises from the three isoforms of Cav3 channels: Cav3.1, Cav3.2, and Cav3.3. From pharmacological analysis of the recombinant T-type channels, low concentrations (

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Bibliographic Details
Published in:The Journal of biological chemistry 2006-02, Vol.281 (8), p.4823-4830
Main Authors: Kang, Ho-Won, Park, Jin-Yong, Jeong, Seong-Woo, Kim, Jin-Ah, Moon, Hyung-Jo, Perez-Reyes, Edward, Lee, Jung-Ha
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Binding Sites
Calcium Channels, T-Type - chemistry
Calcium Channels, T-Type - genetics
Calcium Channels, T-Type - physiology
Cloning, Molecular
Electrophysiology
Histidine - chemistry
Humans
Hydrogen-Ion Concentration
Inhibitory Concentration 50
Ions
Kinetics
Molecular Sequence Data
Mutagenesis, Site-Directed
Mutation
Nickel - chemistry
Nickel - pharmacology
Oocytes - metabolism
Plasmids - metabolism
Point Mutation
Protein Binding
Protein Isoforms
Protein Structure, Tertiary
Recombinant Fusion Proteins - chemistry
Recombinant Fusion Proteins - metabolism
Recombinant Proteins - chemistry
RNA, Complementary - metabolism
Sequence Homology, Amino Acid
Xenopus
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Description
Summary:Molecular cloning studies have revealed that heterogeneity of T-type Ca2+ currents in native tissues arises from the three isoforms of Cav3 channels: Cav3.1, Cav3.2, and Cav3.3. From pharmacological analysis of the recombinant T-type channels, low concentrations (
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M510197200