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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2000-7-10
pubmed:abstractText
Voltage-dependent K+ channels open when depolarizing the membrane voltage. Among the different alpha-subunits, the time course of current activation spreads over a wide range. The structural basis underlying this diversity is not known. We constructed multiple chimeras between two voltage-dependent K+ channels, the rapidly activating Kv1.2 and the slowly activating Kv2.1, and we focused on the C-terminal half of the core region. The general strategy was to substitute parts of Kv2.1 by corresponding parts of Kv1.2 and to test for an acceleration of activation. We identified three regions which contribute to the determination of the activation kinetics: the S5-pore linker, the deep pore, and the S4-segment.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1060-6823
pubmed:author
pubmed:issnType
Print
pubmed:volume
7
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
65-75
pubmed:dateRevised
2005-11-17
pubmed:meshHeading
pubmed:year
2000
pubmed:articleTitle
Structural elements determining activation kinetics in Kv2.1.
pubmed:affiliation
Institut für Physiologie, Herz-Kreislauf-Physiologie, Friedrich-Schiller-Universität, Jena, Germany.
pubmed:publicationType
Journal Article