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

@article{citeulike:1186309, 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.}, address = {Howard Hughes Medical Institute, Laboratory of Molecular Neurobiology and Biophysics, The Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.}, author = {Lee, S. Y. and Lee, A. and Chen, J. and MacKinnon, R. }, citeulike-article-id = {1186309}, doi = {http://dx.doi.org/10.1073/pnas.0507651102}, issn = {0027-8424}, journal = {Proc Natl Acad Sci U S A}, keywords = {antibody\_crystallization, crystallization, xtal\_methods}, month = {October}, number = {43}, pages = {15441--15446}, posted-at = {2007-03-25 19:04:34}, priority = {2}, title = {Structure of the KvAP voltage-dependent K+ channel and its dependence on the lipid membrane.}, url = {http://dx.doi.org/10.1073/pnas.0507651102}, volume = {102}, year = {2005} }

TY - JOUR ID - citeulike:1186309 L3 - citeulike-article-id:1186309 N2 - 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. IS - 43 JF - Proc Natl Acad Sci U S A SN - 0027-8424 AD - Howard Hughes Medical Institute, Laboratory of Molecular Neurobiology and Biophysics, The Rockefeller University, 1230 York Avenue, New York, NY 10021, USA. EP - 15446 TI - Structure of the KvAP voltage-dependent K+ channel and its dependence on the lipid membrane. VL - 102 SP - 15441 KW - antibody_crystallization KW - crystallization KW - xtal_methods AU - Lee, SY AU - Lee, A AU - Chen, J AU - MacKinnon, R PY - 2005/10/25/ UR - http://dx.doi.org/10.1073/pnas.0507651102 ER -