Cation-selective mutations in the M2 domain of the inhibitory glycine receptor channel reveal determinants of ion-charge selectivity

Journal of General Physiology

Volumn 119, Issue 5, 2002, Pages 393-410

  Keramidas, Angelo ^a   Moorhouse, Andrew J ^b   Pierce, Kerrie D ^a   Schofield, Peter R ^b   Barry, Peter H ^a  

^a UNIVERSITY OF NEW SOUTH WALES   (Australia)

^b GARVAN INSTITUTE OF MEDICAL RESEARCH   (Australia)

Author keywords

Electrostatics; Ligand gated ion channels; Permeability; Pore diameter; Selectivity filter

Indexed keywords

CALCIUM; CATION; GLYCINE RECEPTOR; ION; ION CHANNEL; GLYCINE RECEPTOR ALPHA1; LIGAND;

ARTICLE; CALCIUM TRANSPORT; CHANNEL GATING; ELECTRICITY; ELECTROPHYSIOLOGY; FILTER; HUMAN; HUMAN CELL; MUTATION; PERMEABILITY; PROTEIN ANALYSIS; PROTEIN DOMAIN; AMINO ACID SEQUENCE; CELL LINE; CELL MEMBRANE PERMEABILITY; CHEMISTRY; GENETICS; METABOLISM; MOLECULAR GENETICS; NERVE CELL INHIBITION; PHYSIOLOGY; POINT MUTATION; SITE DIRECTED MUTAGENESIS;

AMINO ACID SEQUENCE; CALCIUM; CATIONS; CELL LINE; CELL MEMBRANE PERMEABILITY; HUMAN; ION CHANNEL GATING; LIGANDS; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; NEURAL INHIBITION; POINT MUTATION; RECEPTORS, GLYCINE; SUPPORT, NON-U.S. GOV'T; HUMANS;

EID: 0035999831     PISSN: 00221295     EISSN: None     Source Type: Journal    
DOI: 10.1085/jgp.20028552     Document Type: Article

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