title: Structural basis of ion channel permeation and selectivity.
abstract: There has been rapid progress in understanding the structural basis of ion selectivity and permeation in both ligand- and voltage-gated channels. Recognition of similarities in overall architecture within a channel class has led to an increasing focus on the specific molecular determinants that endow a channel with its own distinctive character. It has been possible in some cases to identify individual amino acids essential for ion selectivity.
authors.affiliation: Beckman Center, Department of Molecular and Cellular Physiology, Stanford University Medical Center, California 94305.
authors.forename: W A
authors.initials: WA
authors.lastname: Sather
authors.forename: J
authors.initials: J
authors.lastname: Yang
authors.forename: R W
authors.initials: RW
authors.lastname: Tsien
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D000838:Anions / Q000378:metabolism; D015220:Calcium Channels / Q000235:genetics / Q000378:metabolism; D016384:Consensus Sequence; D006801:Humans; D015640:Ion Channel Gating; D007473:Ion Channels / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data; D018377:Neurotransmitter Agents / Q000502:physiology; D009712:Nucleotides, Cyclic / Q000502:physiology; D010539:Permeability; D015221:Potassium Channels / Q000235:genetics / Q000378:metabolism; D015222:Sodium Channels / Q000235:genetics / Q000378:metabolism
chemical_list: D000838:Anions; D015220:Calcium Channels; D007473:Ion Channels; D018377:Neurotransmitter Agents; D009712:Nucleotides, Cyclic; D015221:Potassium Channels; D015222:Sodium Channels