AbstractGlutamic acid residues in the SS2 segment of the internal repeats III and IV of the brain calcium channel BI were subjected to single point mutations. The mutant channels were tested for macroscopic current properties and sensitivities to inorganic blockers. The mutation that replaces glutamic acid 1,469 with glutamine altered ion-selection properties and strongly reduced the sensitivity to Cd2+, whereas the analogous mutation of glutamic acid 1,765 exerted smaller effects on ion-selection properties. Our results indicate that these glutamic acid residues, equivalently positioned in the aligned sequences, play different roles in the selective permeability of the calcium channel
Ion channel selectivity is essential for their function, yet the molecular basis of a channel's abil...
AbstractSmall-conductance Ca2+-activated potassium channels (SKCa channels) are heteromeric complexe...
Abstract Single point mutations in pore-forming S6 seg-ments of calcium channels may transform a hig...
Voltage-sensitive sodium channels and calcium channels are homologous proteins with distinctly diffe...
A conserved lysine residue in the "P loop" of domain III renders sodium channels highly selective. C...
AbstractThe mechanisms underlying ion transport and selectivity in calcium channels are examined usi...
AbstractCa2+ channels display remarkable selectivity and permeability, traditionally attributed to m...
A conserved lysine residue in the "P loop" of domain III renders sodium channels highly selective. C...
AbstractHigh-affinity, intrapore binding of Ca2+ over competing ions is the essential feature in the...
AbstractHigh-affinity, intrapore binding of Ca2+ over competing ions is the essential feature in the...
Abstract Voltage-dependent L-type Ca2 ' channels select for Ca2 ' and other divalent catio...
AbstractBa2+ currents through CaV1.2 Ca2+ channels are typically twice as large as Ca2+ currents. Re...
The high-conductance Ca2+-activated K+ channel (mSlo) plays a vital role in regulating calcium entry...
AbstractWe propose a model of calcium channels that can explain most of their observed properties, i...
AbstractCa2+ channels display remarkable selectivity and permeability, traditionally attributed to m...
Ion channel selectivity is essential for their function, yet the molecular basis of a channel's abil...
AbstractSmall-conductance Ca2+-activated potassium channels (SKCa channels) are heteromeric complexe...
Abstract Single point mutations in pore-forming S6 seg-ments of calcium channels may transform a hig...
Voltage-sensitive sodium channels and calcium channels are homologous proteins with distinctly diffe...
A conserved lysine residue in the "P loop" of domain III renders sodium channels highly selective. C...
AbstractThe mechanisms underlying ion transport and selectivity in calcium channels are examined usi...
AbstractCa2+ channels display remarkable selectivity and permeability, traditionally attributed to m...
A conserved lysine residue in the "P loop" of domain III renders sodium channels highly selective. C...
AbstractHigh-affinity, intrapore binding of Ca2+ over competing ions is the essential feature in the...
AbstractHigh-affinity, intrapore binding of Ca2+ over competing ions is the essential feature in the...
Abstract Voltage-dependent L-type Ca2 ' channels select for Ca2 ' and other divalent catio...
AbstractBa2+ currents through CaV1.2 Ca2+ channels are typically twice as large as Ca2+ currents. Re...
The high-conductance Ca2+-activated K+ channel (mSlo) plays a vital role in regulating calcium entry...
AbstractWe propose a model of calcium channels that can explain most of their observed properties, i...
AbstractCa2+ channels display remarkable selectivity and permeability, traditionally attributed to m...
Ion channel selectivity is essential for their function, yet the molecular basis of a channel's abil...
AbstractSmall-conductance Ca2+-activated potassium channels (SKCa channels) are heteromeric complexe...
Abstract Single point mutations in pore-forming S6 seg-ments of calcium channels may transform a hig...