Structural determinants of the high affinity extracellular zinc binding site on Cav3.2 T-type calcium channels.

doi:10.1074/jbc.M109.067660

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Article

Structural determinants of the high affinity extracellular zinc binding site on Cav3.2 T-type calcium channels.

The Journal of biological chemistry - 29 Jan 2010

Kang Ho-Won, Vitko Iuliia, Lee Sang-Soo, Perez-Reyes Edward, Lee Jung-Ha

Abstract excerpt

Ca(v)3.2 T-type channels contain a high affinity metal binding site for trace metals such as copper and zinc. This site is occupied at physiologically relevant concentrations of these metals, leading to decreased channel activity and pain transmission. A histidine at position 191 was recently identified as a critical determinant for both trace metal block of Ca(v)3.2 and modulation by redox agents. His(191) is...

Topics

Animals
Aspartic Acid
Binding Sites
Calcium Channels, T-Type
Electrophysiology
Female
Histidine
Inhibitory Concentration 50
Models, Molecular
Mutation
Oocytes
Oxidation-Reduction
Rats
Xenopus
Zinc

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Identifiers

PMID: 19940152
DOI: 10.1074/jbc.M109.067660
PMCID: PMC2823403

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