Structural Insights into the Functional Interaction of KChIP1 with Shal-Type K + Channels
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 Å crystal structure of the co...
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| Veröffentlicht in: | Neuron (Cambridge, Mass.) Mass.), 2004-02, Vol.41 (4), p.573-586 |
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| creator | Zhou, Wei Qian, Yan Kunjilwar, Kumud Pfaffinger, Paul J. Choe, Senyon |
| description | 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 Å 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 α helix (α1) and the C-terminal α helix (H10) of KChIP1 are enclosed nearly coaxially by these shells. As a result, the H10 of KChIP1 and α1 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 α1 and H10 are essential to the modulation of Kv4.2 by KChIPs. |
| doi_str_mv | 10.1016/S0896-6273(04)00045-5 |
| format | Article |
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Here we report a 2.0 Å 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 α helix (α1) and the C-terminal α helix (H10) of KChIP1 are enclosed nearly coaxially by these shells. As a result, the H10 of KChIP1 and α1 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 α1 and H10 are essential to the modulation of Kv4.2 by KChIPs.</description><identifier>ISSN: 0896-6273</identifier><identifier>EISSN: 1097-4199</identifier><identifier>DOI: 10.1016/S0896-6273(04)00045-5</identifier><identifier>PMID: 14980206</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Animals ; Binding Sites - genetics ; Calcium - metabolism ; Calcium-Binding Proteins - chemistry ; Calcium-Binding Proteins - genetics ; Calcium-Binding Proteins - metabolism ; Cell Membrane - chemistry ; Cell Membrane - genetics ; Cell Membrane - metabolism ; CHO Cells ; COS Cells ; Cricetinae ; Crystallography, X-Ray ; Dimerization ; Hands ; Heart ; Kinases ; Kv Channel-Interacting Proteins ; Ligands ; Membrane Potentials - genetics ; Models, Molecular ; Molecular Sequence Data ; Mutagenesis, Site-Directed - genetics ; Phenylalanine - metabolism ; Potassium Channels - chemistry ; Potassium Channels - genetics ; Potassium Channels - metabolism ; Potassium Channels, Voltage-Gated ; Protein Structure, Secondary - genetics ; Protein Structure, Tertiary - genetics ; Protein Subunits - chemistry ; Protein Subunits - genetics ; Protein Subunits - metabolism ; Proteins ; Rats ; Sequence Homology, Amino Acid ; Shal Potassium Channels ; Signal transduction ; Tryptophan - metabolism</subject><ispartof>Neuron (Cambridge, Mass.), 2004-02, Vol.41 (4), p.573-586</ispartof><rights>2004 Cell Press</rights><rights>Copyright Elsevier Limited Feb 19, 2004</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c488t-65486c1b06eb2975d1d540d384eb0619432bc32b0444d04762386c1609300a8d3</citedby><cites>FETCH-LOGICAL-c488t-65486c1b06eb2975d1d540d384eb0619432bc32b0444d04762386c1609300a8d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0896627304000455$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,776,780,3536,27903,27904,65309</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/14980206$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Zhou, Wei</creatorcontrib><creatorcontrib>Qian, Yan</creatorcontrib><creatorcontrib>Kunjilwar, Kumud</creatorcontrib><creatorcontrib>Pfaffinger, Paul J.</creatorcontrib><creatorcontrib>Choe, Senyon</creatorcontrib><title>Structural Insights into the Functional Interaction of KChIP1 with Shal-Type K + Channels</title><title>Neuron (Cambridge, Mass.)</title><addtitle>Neuron</addtitle><description>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 Å 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 α helix (α1) and the C-terminal α helix (H10) of KChIP1 are enclosed nearly coaxially by these shells. As a result, the H10 of KChIP1 and α1 of Kv4.2 mediate interactions between these two molecules, structurally reminiscent of the interactions between calmodulin and its target peptides. 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Here we report a 2.0 Å 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 α helix (α1) and the C-terminal α helix (H10) of KChIP1 are enclosed nearly coaxially by these shells. As a result, the H10 of KChIP1 and α1 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 α1 and H10 are essential to the modulation of Kv4.2 by KChIPs.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>14980206</pmid><doi>10.1016/S0896-6273(04)00045-5</doi><tpages>14</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Animals Binding Sites - genetics Calcium - metabolism Calcium-Binding Proteins - chemistry Calcium-Binding Proteins - genetics Calcium-Binding Proteins - metabolism Cell Membrane - chemistry Cell Membrane - genetics Cell Membrane - metabolism CHO Cells COS Cells Cricetinae Crystallography, X-Ray Dimerization Hands Heart Kinases Kv Channel-Interacting Proteins Ligands Membrane Potentials - genetics Models, Molecular Molecular Sequence Data Mutagenesis, Site-Directed - genetics Phenylalanine - metabolism Potassium Channels - chemistry Potassium Channels - genetics Potassium Channels - metabolism Potassium Channels, Voltage-Gated Protein Structure, Secondary - genetics Protein Structure, Tertiary - genetics Protein Subunits - chemistry Protein Subunits - genetics Protein Subunits - metabolism Proteins Rats Sequence Homology, Amino Acid Shal Potassium Channels Signal transduction Tryptophan - metabolism |
| title | Structural Insights into the Functional Interaction of KChIP1 with Shal-Type K + Channels |
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