The carboxyl-terminal region of cyclic nucleotide-modulated channels is a gating ring, not a permeation path

Proceedings of the National Academy of Sciences of the United States of America

Volumn 102, Issue 8, 2005, Pages 2742-2747

  Johnson Jr , J P ^a   Zagotta, William N ^a  

^a UNIVERSITY OF WASHINGTON SCHOOL OF MEDICINE   (United States)

Author keywords

Charge ring; Cyclic nucleotide gate; Fluctuation analysis; Hyperpolarization activated cyclic nucleotide modulated; Single channel patch clamp

Indexed keywords

AMINO ACID; CYCLIC NUCLEOTIDE; CYSTEINE; VOLTAGE GATED POTASSIUM CHANNEL;

ANIMAL CELL; ARTICLE; CARBOXY TERMINAL SEQUENCE; CELL MEMBRANE PERMEABILITY; CHANNEL GATING; CRYSTAL STRUCTURE; CYCLIC NUCLEOTIDE GATED CHANNEL; CYCLIC NUCLEOTIDE MODULATED CHANNEL; HYPERPOLARIZATION; MEMBRANE CHANNEL; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN STRUCTURE; XENOPUS LAEVIS;

AMINO ACID SEQUENCE; ANIMALS; ELECTRIC CONDUCTIVITY; ION CHANNEL GATING; ION CHANNELS; MOLECULAR SEQUENCE DATA; MUSCLE PROTEINS; PERMEABILITY; XENOPUS LAEVIS;

EID: 14544271928     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0408323102     Document Type: Article

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