Change of pore helix conformational state upon opening of cyclic nucleotide-gated channels. Export

@article{citeulike:5969034, abstract = {The structure of the pore region of the alpha subunit of the bovine rod cyclic nucleotide-gated channel was probed using cysteine-scanning mutagenesis and hydrophilic sulfhydryl-reactive methanethiosulfonate (MTS) reagents. A region homologous to the pore helix in the X-ray crystal structure of the KcsA K(+) channel showed a helical pattern of reactivity with externally applied MTS reagents. Surprisingly, three out of four of the reactive residues, all on one face of the pore helix, only reacted with MTS reagents in the closed state. A residue on the opposite face of the helix only reacted with MTS reagents in the open state. These results indicate that the pore helix (or its surroundings) undergoes a change in conformation, perhaps involving a rotation around its long axis, that opens a gate localized to the selectivity filter of the channel.}, author = {Liu, J. and Siegelbaum, S. A.}, citeulike-article-id = {5969034}, citeulike-linkout-0 = {http://view.ncbi.nlm.nih.gov/pubmed/11163275}, citeulike-linkout-1 = {http://www.hubmed.org/display.cgi?uids=11163275}, issn = {0896-6273}, journal = {Neuron}, keywords = {kcsa, open-closed, pore}, month = {December}, number = {3}, pages = {899--909}, posted-at = {2009-10-19 05:51:03}, priority = {2}, title = {Change of pore helix conformational state upon opening of cyclic nucleotide-gated channels.}, url = {http://view.ncbi.nlm.nih.gov/pubmed/11163275}, volume = {28}, year = {2000} }

TY - JOUR ID - citeulike:5969034 L3 - citeulike-article-id:5969034 N2 - The structure of the pore region of the alpha subunit of the bovine rod cyclic nucleotide-gated channel was probed using cysteine-scanning mutagenesis and hydrophilic sulfhydryl-reactive methanethiosulfonate (MTS) reagents. A region homologous to the pore helix in the X-ray crystal structure of the KcsA K(+) channel showed a helical pattern of reactivity with externally applied MTS reagents. Surprisingly, three out of four of the reactive residues, all on one face of the pore helix, only reacted with MTS reagents in the closed state. A residue on the opposite face of the helix only reacted with MTS reagents in the open state. These results indicate that the pore helix (or its surroundings) undergoes a change in conformation, perhaps involving a rotation around its long axis, that opens a gate localized to the selectivity filter of the channel. IS - 3 JF - Neuron SN - 0896-6273 EP - 909 TI - Change of pore helix conformational state upon opening of cyclic nucleotide-gated channels. VL - 28 SP - 899 KW - kcsa KW - open-closed KW - pore AU - Liu, J AU - Siegelbaum, SA PY - 2000/12// UR - http://view.ncbi.nlm.nih.gov/pubmed/11163275 ER -