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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
2004-2-24
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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.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Kcnd1 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Kcnd2 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Kcnip1 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Kv Channel-Interacting Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phenylalanine,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium Channels,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium Channels, Voltage-Gated,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Subunits,
http://linkedlifedata.com/resource/pubmed/chemical/Shal Potassium Channels,
http://linkedlifedata.com/resource/pubmed/chemical/Tryptophan
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0896-6273
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
19
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pubmed:volume |
41
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
573-86
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:14980206-Animals,
pubmed-meshheading:14980206-Binding Sites,
pubmed-meshheading:14980206-CHO Cells,
pubmed-meshheading:14980206-COS Cells,
pubmed-meshheading:14980206-Calcium,
pubmed-meshheading:14980206-Calcium-Binding Proteins,
pubmed-meshheading:14980206-Cell Membrane,
pubmed-meshheading:14980206-Cricetinae,
pubmed-meshheading:14980206-Crystallography, X-Ray,
pubmed-meshheading:14980206-Dimerization,
pubmed-meshheading:14980206-Kv Channel-Interacting Proteins,
pubmed-meshheading:14980206-Membrane Potentials,
pubmed-meshheading:14980206-Models, Molecular,
pubmed-meshheading:14980206-Molecular Sequence Data,
pubmed-meshheading:14980206-Mutagenesis, Site-Directed,
pubmed-meshheading:14980206-Phenylalanine,
pubmed-meshheading:14980206-Potassium Channels,
pubmed-meshheading:14980206-Potassium Channels, Voltage-Gated,
pubmed-meshheading:14980206-Protein Structure, Secondary,
pubmed-meshheading:14980206-Protein Structure, Tertiary,
pubmed-meshheading:14980206-Protein Subunits,
pubmed-meshheading:14980206-Rats,
pubmed-meshheading:14980206-Sequence Homology, Amino Acid,
pubmed-meshheading:14980206-Shal Potassium Channels,
pubmed-meshheading:14980206-Tryptophan
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pubmed:year |
2004
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pubmed:articleTitle |
Structural insights into the functional interaction of KChIP1 with Shal-type K(+) channels.
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pubmed:affiliation |
Division of Neuroscience, Baylor College of Medicine, Houston, TX 77030 USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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