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| Article Authors: | Seok-Yong Lee; Alice Lee; Jiayun Chen; Roderick MacKinnon |
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| Article Title: | Structure of the KvAP voltage-dependent K+ channel and its dependence on the lipid membrane. |
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| Reference ID: | 1002489 |
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| Abstract: | Voltage-dependent ion channels gate open in response to changes in cell membrane voltage. This form of gating permits the propagation of action potentials. We present two structures of the voltage-dependent K(+) channel KvAP, in complex with monoclonal Fv fragments (3.9 A) and without antibody fragments (8 A). We also studied KvAP with disulfide cross-bridges in lipid membranes. Analyzing these data in the context of the crystal structure of Kv1.2 and EPR data on KvAP we reach the following conclusions: (i) KvAP is similar in structure to Kv1.2 with a very modest difference in the orientation of its voltage sensor; (ii) mAb fragments are not the source of non-native conformations of KvAP in crystal structures; (iii) because KvAP contains separate loosely adherent domains, a lipid membrane is required to maintain their correct relative orientations, and (iv) the model of KvAP is consistent with the proposal of voltage sensing through the movement of an arginine-containing helix-turn-helix element at the protein-lipid interface. |
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| Affiliations: | Howard Hughes Medical Institute, Laboratory of Molecular Neurobiology and Biophysics, The Rockefeller University, 1230 York Avenue, New York, NY 10021, USA. |
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| Date: | 2005 |
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| Reference Type: | Literature |
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| PubMed ID: | 16223877 |
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| Journal: | Proc Natl Acad Sci U S A |
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| Journal Volume: | 102 |
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| Article Pages: | 15441-6 |
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| Journal ISSN: | 1091-6490 |
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| Article Chemical List: | Kv1.2 Potassium Channel;Lipid Bilayers;Membrane Lipids;Potassium Channels, Voltage-Gated |
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| Article MeSH List: | Crystallization; Kv1.2 Potassium Channel(chemistry); Lipid Bilayers(chemistry); Membrane Lipids(chemistry); Potassium Channels, Voltage-Gated(chemistry); Protein Conformation |
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| Curation Last Updated: | 2013-05-28 20:35:10 |
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