Epitopes described in "Structure of the KvAP voltage-dependent K+ channel and its dependence on the lipid membrane."

Article Authors:Seok-Yong Lee; Alice Lee; Jiayun Chen; Roderick MacKinnon
Article Title:Structure of the KvAP voltage-dependent K+ channel and its dependence on the lipid membrane.
Reference Detail
Reference ID:1002489
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.
Affiliations:Howard Hughes Medical Institute, Laboratory of Molecular Neurobiology and Biophysics, The Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.
Reference Type:Literature
PubMed ID:16223877
Journal:Proc Natl Acad Sci U S A
Journal Volume:102
Article Pages:15441-6
Journal ISSN:0027-8424
Article Chemical List:Kv1.2 Potassium Channel;Lipid Bilayers;Membrane Lipids;Potassium Channels, Voltage-Gated
Article MeSH List:Crystallization; Kv1.2 Potassium Channel(chemistry); Lipid Bilayers(chemistry); Membrane Lipids(chemistry); Potassium Channels, Voltage-Gated(chemistry); Protein Conformation
Curation Last Updated:2015-06-05 00:41:22