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Structure of three high voltage-activated calcium channel α1 subunits from Schistosoma mansoni

Published online by Cambridge University Press:  06 February 2003

A. B. KOHN
Affiliation:
Whitney Laboratory, University of Florida, 9505 Ocean Shore Blvd, St Augustine FL 32080, USA
J. M. LEA
Affiliation:
Whitney Laboratory, University of Florida, 9505 Ocean Shore Blvd, St Augustine FL 32080, USA
J. M. ROBERTS-MISTERLY
Affiliation:
Whitney Laboratory, University of Florida, 9505 Ocean Shore Blvd, St Augustine FL 32080, USA
P. A. V. ANDERSON
Affiliation:
Whitney Laboratory, University of Florida, 9505 Ocean Shore Blvd, St Augustine FL 32080, USA Department of Neuroscience, University of Florida, 9505 Ocean Shore Blvd, St Augustine FL 32080, USA Department of Physiology, University of Florida, 9505 Ocean Shore Blvd, St Augustine FL 32080, USA
R. M. GREENBERG
Affiliation:
Whitney Laboratory, University of Florida, 9505 Ocean Shore Blvd, St Augustine FL 32080, USA Department of Neuroscience, University of Florida, 9505 Ocean Shore Blvd, St Augustine FL 32080, USA

Abstract

Voltage-gated calcium (Ca2+) channels contribute to impulse propagation in excitable cells and also regulate intracellular levels of Ca2+. High voltage-activated (HVA) Ca2+ channels are heteromultimeric membrane proteins. The pore-forming, voltage-sensing subunit is the α1 subunit. We have cloned 3 HVA Ca2+ channel α1 subunit cDNAs from Schistosoma mansoni. One of these sequences most closely resembles the L-type class of HVA α1 subunits. The other two sequences are most closely related to non L-type α1 subunits. These schistosome α1 subunits have many of the features common to HVA Ca2+ channels, but also have distinct structural motifs. Analysis of the structural and functional properties of schistosome Ca2+ channel subunits may provide information about these critical components of excitable cells.

Type
Research Article
Copyright
© 2001 Cambridge University Press

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