title: Annexin V: the key to understanding ion selectivity and voltage regulation?
abstract: Annexin V is a Ca(2+)-dependent membrane-binding protein that forms voltage-dependent Ca2+ channels in phospholipid bilayers and is the first ion channel to be structurally and functionally characterized. Data outlined here indicate that key amino acid residues act as selectivity filters and voltage sensors, thereby regulating the permeability of the channel pore to ions.
authors.affiliation: Abteilung Strukturforschung, Max Planck Institut für Biochemie, Martinsried, Germany.
authors.forename: P
authors.initials: P
authors.lastname: Demange
authors.forename: D
authors.initials: D
authors.lastname: Voges
authors.forename: J
authors.initials: J
authors.lastname: Benz
authors.forename: S
authors.initials: S
authors.lastname: Liemann
authors.forename: P
authors.initials: P
authors.lastname: Göttig
authors.forename: R
authors.initials: R
authors.lastname: Berendes
authors.forename: A
authors.initials: A
authors.lastname: Burger
authors.forename: R
authors.initials: R
authors.lastname: Huber
mesh_terms: D017304:Annexin A5 / Q000737:chemistry / Q000502:physiology*; D015220:Calcium Channels / Q000737:chemistry / Q000502:physiology; D002462:Cell Membrane / Q000502:physiology; D004252:DNA Mutational Analysis; D006801:Humans; D015640:Ion Channel Gating; D007473:Ion Channels / Q000502:physiology*; D009154:Mutation; D011487:Protein Conformation; D013329:Structure-Activity Relationship
chemical_list: D017304:Annexin A5; D015220:Calcium Channels; D007473:Ion Channels