| pubmed-article:11723128 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11723128 | lifeskim:mentions | umls-concept:C0205147 | lld:lifeskim |
| pubmed-article:11723128 | lifeskim:mentions | umls-concept:C0949653 | lld:lifeskim |
| pubmed-article:11723128 | lifeskim:mentions | umls-concept:C2587213 | lld:lifeskim |
| pubmed-article:11723128 | lifeskim:mentions | umls-concept:C1879748 | lld:lifeskim |
| pubmed-article:11723128 | lifeskim:mentions | umls-concept:C1706853 | lld:lifeskim |
| pubmed-article:11723128 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:11723128 | pubmed:dateCreated | 2002-2-4 | lld:pubmed |
| pubmed-article:11723128 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11723128 | 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. | lld:pubmed |
| pubmed-article:11723128 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11723128 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11723128 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11723128 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11723128 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11723128 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11723128 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11723128 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11723128 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11723128 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:11723128 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:11723128 | pubmed:author | pubmed-author:WissmannRalph... | lld:pubmed |
| pubmed-article:11723128 | pubmed:author | pubmed-author:BildlWolfgang... | lld:pubmed |
| pubmed-article:11723128 | pubmed:author | pubmed-author:NeumannHeinzH | lld:pubmed |
| pubmed-article:11723128 | pubmed:author | pubmed-author:RivardAndre... | lld:pubmed |
| pubmed-article:11723128 | pubmed:author | pubmed-author:KlöckerNikola... | lld:pubmed |
| pubmed-article:11723128 | pubmed:author | pubmed-author:WeitzDietmarD | lld:pubmed |
| pubmed-article:11723128 | pubmed:author | pubmed-author:SchulteUweU | lld:pubmed |
| pubmed-article:11723128 | pubmed:author | pubmed-author:AdelmanJohn... | lld:pubmed |
| pubmed-article:11723128 | pubmed:author | pubmed-author:BentropDetlef... | lld:pubmed |
| pubmed-article:11723128 | pubmed:author | pubmed-author:FaklerBerndB | lld:pubmed |
| pubmed-article:11723128 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11723128 | pubmed:day | 8 | lld:pubmed |
| pubmed-article:11723128 | pubmed:volume | 277 | lld:pubmed |
| pubmed-article:11723128 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11723128 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11723128 | pubmed:pagination | 4558-64 | lld:pubmed |
| pubmed-article:11723128 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:11723128 | pubmed:meshHeading | pubmed-meshheading:11723128... | lld:pubmed |
| pubmed-article:11723128 | pubmed:meshHeading | pubmed-meshheading:11723128... | lld:pubmed |
| pubmed-article:11723128 | pubmed:meshHeading | pubmed-meshheading:11723128... | lld:pubmed |
| pubmed-article:11723128 | pubmed:meshHeading | pubmed-meshheading:11723128... | lld:pubmed |
| pubmed-article:11723128 | pubmed:meshHeading | pubmed-meshheading:11723128... | lld:pubmed |
| pubmed-article:11723128 | pubmed:meshHeading | pubmed-meshheading:11723128... | lld:pubmed |
| pubmed-article:11723128 | pubmed:meshHeading | pubmed-meshheading:11723128... | lld:pubmed |
| pubmed-article:11723128 | pubmed:meshHeading | pubmed-meshheading:11723128... | lld:pubmed |
| pubmed-article:11723128 | pubmed:meshHeading | pubmed-meshheading:11723128... | lld:pubmed |
| pubmed-article:11723128 | pubmed:meshHeading | pubmed-meshheading:11723128... | lld:pubmed |
| pubmed-article:11723128 | pubmed:meshHeading | pubmed-meshheading:11723128... | lld:pubmed |
| pubmed-article:11723128 | pubmed:meshHeading | pubmed-meshheading:11723128... | lld:pubmed |
| pubmed-article:11723128 | pubmed:meshHeading | pubmed-meshheading:11723128... | lld:pubmed |
| pubmed-article:11723128 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:11723128 | pubmed:articleTitle | A helical region in the C terminus of small-conductance Ca2+-activated K+ channels controls assembly with apo-calmodulin. | lld:pubmed |
| pubmed-article:11723128 | pubmed:affiliation | Department of Physiology II, University of Tübingen, Ob dem Himmelreich 7, 72074 Tübingen, Germany. | lld:pubmed |
| pubmed-article:11723128 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11723128 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11723128 | lld:pubmed |
