Structure-Function Relationship
of K+ Ion Channel Toxins
From Cloning to Functional Characterization
Acta Biomedica Lovaniensia, No. 305

By Isabelle Huys
April 2004
Leuven University Press
ISBN: 90-5867-353-7
177 pages, Illustrated, 6 ¼" x 9 ½"
$99.50 Paper Original

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This is a Ph.D. dissertation. Many fundamental processes underlying nerve and muscle excitation, hormone secretion, learning and memory, cell proliferation, sensory transduction and regulation of blood pressure and osmotic balance, are attributed to a diverse repertoire of membrane proteins, named ion channels, present in all living plant, bacterial and animal cells.

Each cell type selects its own blend of ion channels to suit its special purposes. K+ channels represent the most diverse class of ion channels, with respect to their kinetic properties, regulation and pharmacology.

To date, more than 80 K+ channel-related genes have been cloned and characterized. Based on their fundamental properties and gating properties, K+ channels can be divided in several types: Kv-channels (voltage-activated K+ channels), KCa Channels (Ca2+ -activated K+ channels), Kir-channels (inward rectifier K+ channels) and two-pore K+ channels. Voltage-activated K+ channels belong to a large family of evolutionary related proteins including Na+ channels, Ca2+ channels and others like CNG (cyclic nucleotide-gated) channels.

Biochemistry

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