title: Molecular dynamics simulation approaches to K channels: conformational flexibility and physiological function.
abstract: Molecular modeling and simulations enable extrapolation for the structure of bacterial potassium channels to the function of their mammalian homologues. Molecular dynamics simulations have revealed the concerted single-file motion of potassium ions and water molecules through the selectivity filter of K channels and the role of filter flexibility in ion permeation and in "fast gating." Principal components analysis of extended K channel simulations suggests that hinge-bending of pore-lining M2 (or S6) helices plays a key role in K channel gating. Based on these and other simulations, a molecular model for gating of inward rectifier K channel gating is presented.
authors.affiliation: Department of Biochemistry, University of Oxford, Oxford OX 3QU, United Kingdom. grottesi@biop.ox.ac.uk
authors.forename: Alessandro
authors.initials: A
authors.lastname: Grottesi
authors.forename: Carmen
authors.initials: C
authors.lastname: Domene
authors.forename: Shozeb
authors.initials: S
authors.lastname: Haider
authors.forename: Mark S P
authors.initials: MS
authors.lastname: Sansom
mesh_terms: D000818:Animals; D002462:Cell Membrane / Q000737:chemistry* / Q000502:physiology*; D002463:Cell Membrane Permeability / Q000502:physiology; D006801:Humans; D015640:Ion Channel Gating / Q000502:physiology*; D007700:Kinetics; D008564:Membrane Potentials / Q000502:physiology; D008954:Models, Biological; D008956:Models, Chemical; D009038:Motion; D016062:Porosity; D015221:Potassium Channels / Q000737:chemistry* / Q000502:physiology*; D011487:Protein Conformation; D013329:Structure-Activity Relationship
chemical_list: D015221:Potassium Channels