| pubmed-article:14980206 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:14980206 | lifeskim:mentions | umls-concept:C0205245 | lld:lifeskim |
| pubmed-article:14980206 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:14980206 | lifeskim:mentions | umls-concept:C0233820 | lld:lifeskim |
| pubmed-article:14980206 | lifeskim:mentions | umls-concept:C1423551 | lld:lifeskim |
| pubmed-article:14980206 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:14980206 | lifeskim:mentions | umls-concept:C0439799 | lld:lifeskim |
| pubmed-article:14980206 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:14980206 | pubmed:dateCreated | 2004-2-24 | lld:pubmed |
| pubmed-article:14980206 | pubmed:abstractText | Four Kv channel-interacting proteins (KChIP1 through KChIP4) interact directly with the N-terminal domain of three Shal-type voltage-gated potassium channels (Kv4.1, Kv4.2, and Kv4.3) to modulate cell surface expression and function of Kv4 channels. Here we report a 2.0 Angstrom crystal structure of the core domain of KChIP1 (KChIP1*) in complex with the N-terminal fragment of Kv4.2 (Kv4.2N30). The complex reveals a clam-shaped dimeric assembly. Four EF-hands from each KChIP1 form each shell of the clam. The N-terminal end of Kv4.2 forming an alpha helix (alpha1) and the C-terminal alpha helix (H10) of KChIP1 are enclosed nearly coaxially by these shells. As a result, the H10 of KChIP1 and alpha1 of Kv4.2 mediate interactions between these two molecules, structurally reminiscent of the interactions between calmodulin and its target peptides. Site-specific mutagenesis combined with functional characterization shows that those interactions mediated by alpha1 and H10 are essential to the modulation of Kv4.2 by KChIPs. | lld:pubmed |
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| pubmed-article:14980206 | pubmed:language | eng | lld:pubmed |
| pubmed-article:14980206 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14980206 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:14980206 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:14980206 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:14980206 | pubmed:issn | 0896-6273 | lld:pubmed |
| pubmed-article:14980206 | pubmed:author | pubmed-author:ZhouWeiW | lld:pubmed |
| pubmed-article:14980206 | pubmed:author | pubmed-author:ChoeSenyonS | lld:pubmed |
| pubmed-article:14980206 | pubmed:author | pubmed-author:PfaffingerPau... | lld:pubmed |
| pubmed-article:14980206 | pubmed:author | pubmed-author:KunjilwarKumu... | lld:pubmed |
| pubmed-article:14980206 | pubmed:author | pubmed-author:QianYanY | lld:pubmed |
| pubmed-article:14980206 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:14980206 | pubmed:day | 19 | lld:pubmed |
| pubmed-article:14980206 | pubmed:volume | 41 | lld:pubmed |
| pubmed-article:14980206 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:14980206 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:14980206 | pubmed:pagination | 573-86 | lld:pubmed |
| pubmed-article:14980206 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:14980206 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:14980206 | pubmed:articleTitle | Structural insights into the functional interaction of KChIP1 with Shal-type K(+) channels. | lld:pubmed |
| pubmed-article:14980206 | pubmed:affiliation | Division of Neuroscience, Baylor College of Medicine, Houston, TX 77030 USA. | lld:pubmed |
| pubmed-article:14980206 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:14980206 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:14980206 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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