Voltage-gated calcium channels (CaVs) are large (∼0.5 MDa), multisubunit, macromolecular machines that control calcium entry into cells in response to membrane potential changes. These molecular switches play pivotal roles in cardiac action potentials, neurotransmitter release, muscle contraction, calcium-dependent gene transcription and synaptic transmission. CaVs possess self-regulatory mechanisms that permit them to change their behaviour in response to activity, including voltage-dependent inactivation, calcium-dependent inactivation and calcium-dependent facilitation. These processes arise from the concerted action of different channel domains with CaV β-subunits and the soluble calcium sensor calmodulin. Until recently, nothing was known about the CaV structure at high resolution. Recent crystallographic work has revealed the first glimpses at the CaV molecular framework and set a new direction towards a detailed mechanistic understanding of CaV function.
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Conference Article|
October 25 2006
The structural biology of voltage-gated calcium channel function and regulation
F. Van Petegem;
F. Van Petegem
1Departments of Biochemistry and Biophysics, and Cellular and Molecular Pharmacology, Cardiovascular Research Institute, California Institute of Quantitative Biomedical Research, University of California San Francisco, San Francisco, CA 94158-2330, U.S.A.
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D.L. Minor, Jr
D.L. Minor, Jr
1
1Departments of Biochemistry and Biophysics, and Cellular and Molecular Pharmacology, Cardiovascular Research Institute, California Institute of Quantitative Biomedical Research, University of California San Francisco, San Francisco, CA 94158-2330, U.S.A.
1To whom correspondence should be addressed (email daniel.minor@ucsf.edu).
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Publisher: Portland Press Ltd
Received:
June 26 2006
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© 2006 The Biochemical Society
2006
Biochem Soc Trans (2006) 34 (5): 887–893.
Article history
Received:
June 26 2006
Citation
F. Van Petegem, D.L. Minor; The structural biology of voltage-gated calcium channel function and regulation. Biochem Soc Trans 1 October 2006; 34 (5): 887–893. doi: https://doi.org/10.1042/BST0340887
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