Source:http://linkedlifedata.com/resource/pubmed/id/11723128
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
2002-2-4
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pubmed:databankReference | |
pubmed:abstractText |
Small conductance Ca(2+)-activated potassium (SK) channels underlie the afterhyperpolarization that follows the action potential in many types of central neurons. SK channels are voltage-independent and gated solely by intracellular Ca(2+) in the submicromolar range. This high affinity for Ca(2+) results from Ca(2+)-independent association of the SK alpha-subunit with calmodulin (CaM), a property unique among the large family of potassium channels. Here we report the solution structure of the calmodulin binding domain (CaMBD, residues 396-487 in rat SK2) of SK channels using NMR spectroscopy. The CaMBD exhibits a helical region between residues 423-437, whereas the rest of the molecule lacks stable overall folding. Disruption of the helical domain abolishes constitutive association of CaMBD with Ca(2+)-free CaM, and results in SK channels that are no longer gated by Ca(2+). The results show that the Ca(2+)-independent CaM-CaMBD interaction, which is crucial for channel function, is at least in part determined by a region different in sequence and structure from other CaM-interacting proteins.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Calmodulin,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium Channels,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium Channels...,
http://linkedlifedata.com/resource/pubmed/chemical/Small-Conductance...
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
8
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pubmed:volume |
277
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4558-64
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:11723128-Amino Acid Sequence,
pubmed-meshheading:11723128-Animals,
pubmed-meshheading:11723128-Calcium,
pubmed-meshheading:11723128-Calmodulin,
pubmed-meshheading:11723128-Immunohistochemistry,
pubmed-meshheading:11723128-Models, Molecular,
pubmed-meshheading:11723128-Molecular Sequence Data,
pubmed-meshheading:11723128-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:11723128-Potassium Channels,
pubmed-meshheading:11723128-Potassium Channels, Calcium-Activated,
pubmed-meshheading:11723128-Protein Conformation,
pubmed-meshheading:11723128-Small-Conductance Calcium-Activated Potassium Channels,
pubmed-meshheading:11723128-Xenopus
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pubmed:year |
2002
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pubmed:articleTitle |
A helical region in the C terminus of small-conductance Ca2+-activated K+ channels controls assembly with apo-calmodulin.
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pubmed:affiliation |
Department of Physiology II, University of Tübingen, Ob dem Himmelreich 7, 72074 Tübingen, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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