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Rings of negatively charged amino acids determine the acetylcholine receptor channel conductance
The single-channel conductance properties of these AChR mutants expressed in Xenopus laevis oocytes indicate that three clusters of negatively charged and glutamine residues neighbouring segment M2 of the α-, β-, γ- and δ-subunits, probably forming three anionic rings, are major determinants of the rate of ion transport. Expand
Primary structure and functional expression from complementary DNA of the rod photoreceptor cyclic GMP-gated channel
The complete amino-acid sequence of the cyclic GMP-gated channel from bovine retinal rod photo-receptors, deduced by cloning and sequencing its complementary DNA, shows that the protein containsExpand
Molecular distinction between fetal and adult forms of muscle acetylcholine receptor
The conductance and gating properties of the two classes of channels suggest that replacement of the γ-subunit by the ε- subunit is responsible for the functional alteration of the receptor during muscle development. Expand
Mapping the site of block by tetrodotoxin and saxitoxin of sodium channel II
The SS2 and adjacent regions of the 4 internal repeats of sodium channel II were subjected to single mutations involving, mainly, charged amino acid residues, showing that mutations involving 2 clusters of predominantly negatively charged residues strongly reduce toxin sensitivity, whereas mutations of adjacent residues exert much smaller or no effects. Expand
Primary structure of the receptor for calcium channel blockers from skeletal muscle
Structural and sequence similarities to the voltage-dependent sodium channel suggest that in the transverse tubule membrane of skeletal muscle the dihydropyridine receptor may act both as voltage sensor in excitation-contraction coupling and as a calcium channel. Expand
Regions of the skeletal muscle dihydropyridine receptor critical for excitation–contraction coupling
The results obtained indicate that the putative cytoplasmic region between repeats II and III of the skeletal muscle DHP receptor3 is an important determinant of skeletal-type EC coupling. Expand
Primary structure of Electrophorus electricus sodium channel deduced from cDNA sequence
Cloning and sequence analysis of cDNA for the Electrophorus electricus electroplax sodium channel indicate that this protein exhibits four repeated homology units, which are presumably oriented in a pseudosymmetric fashion across the membrane. Expand
Calcium channel characteristics conferred on the sodium channel by single mutations
The effects on ion selectivity of replacing lysine at position 1,422 in repeat III and/or alanine in repeat IV of rat sodium channel II are reported, suggesting that these residues constitute part of the selectivity filter of the channel. Expand
Structural parts involved in activation and inactivation of the sodium channel
Evidence is provided that the positive charges in segment S4 are involved in the voltage–sensing mechanism for activation of the channel and that the region between repeats III and IV is important for its inactivation. Expand
Primary structure and functional expression of the cardiac dihydropyridine-sensitive calcium channel
It is shown that messenger RNA derived from the cardiac DHP receptor cDNA is sufficient to direct the formation of a functional DHP-sensitive calcium channel in Xenopus oocytes, and higher calcium-channel activity is observed when mRNA specific for the polypeptide of relative molecular mass associated with the skeletal muscle DHP receptors is co-injected. Expand