Structural determinants of the regulation of the voltage-gated potassium channel Kv2.1 by the Modulatory α-subunit Kv9.3

Journal of Biological Chemistry

Volumn 278, Issue 20, 2003, Pages 18154-18161

  Kerschensteiner, Daniel ^a,b   Monje, Francisco ^a,c   Stocker, Martin ^a,d  

^a MAX PLANCK INSTITUTE OF EXPERIMENTAL MEDICINE   (Germany)

^b UNIVERSITY MEDICAL CENTER GÖTTINGEN   (Germany)

^c Ctro Internacional de Fisica   (Colombia)

^d UNIVERSITY COLLEGE LONDON   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

CELL MEMBRANES; CONFORMATIONS; ELECTRIC POTENTIAL; ENZYME INHIBITION;

VOLTAGE-GATED POTASSIUM (KV) CHANNELS;

CELLS;

MEMBRANE PROTEIN; POTASSIUM ION; PROLINE; PROTEIN KV2 1; PROTEIN KV5; PROTEIN KV6; PROTEIN KV8; PROTEIN KV8 1; PROTEIN KV9; PROTEIN KV9 3; PROTEIN SUBUNIT; TETRYLAMMONIUM; UNCLASSIFIED DRUG; VOLTAGE GATED POTASSIUM CHANNEL; COMPLEMENTARY RNA; DELAYED RECTIFIER POTASSIUM CHANNEL; KCNV1 PROTEIN, MOUSE; NERVE PROTEIN; POTASSIUM; POTASSIUM CHANNEL; SHAB POTASSIUM CHANNEL;

ALPHA CHAIN; AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; CHANNEL GATING; CONTROLLED STUDY; NONHUMAN; OOCYTE; POTASSIUM CELL LEVEL; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN FUNCTION; PROTEIN MOTIF; PROTEIN STRUCTURE; SIGNAL TRANSDUCTION; STRUCTURE ANALYSIS; XENOPUS LAEVIS; AMINO ACID SEQUENCE; ANIMAL; CHEMISTRY; DIMERIZATION; ELECTROPHYSIOLOGY; KINETICS; METABOLISM; MOLECULAR GENETICS; PROTEIN BINDING; PROTEIN TERTIARY STRUCTURE; SITE DIRECTED MUTAGENESIS;

ANIMALIA; XENOPUS LAEVIS;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; ANIMALS; DELAYED RECTIFIER POTASSIUM CHANNELS; DIMERIZATION; ELECTROPHYSIOLOGY; KINETICS; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; NERVE TISSUE PROTEINS; POTASSIUM; POTASSIUM CHANNELS; POTASSIUM CHANNELS, VOLTAGE-GATED; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; RNA, COMPLEMENTARY; SHAB POTASSIUM CHANNELS; TETRAETHYLAMMONIUM; XENOPUS LAEVIS;

EID: 0037705349     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M213117200     Document Type: Article

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