Solution NMR structure of the C-terminal EF-hand domain of human cardiac sodium channel Nav1.5

Journal of Biological Chemistry

Volumn 284, Issue 10, 2009, Pages 6436-6445

  Chagot, Benjamin ^a,b   Potet, Franck ^a   Balser, Jeffrey R ^a   Chazin, Walter J ^a,b  

^a VANDERBILT UNIVERSITY   (United States)

^b VANDERBILT UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTION POTENTIALS; CALCIUM BINDING; CALCIUM BINDING PROTEINS; CALCIUM REGULATION; CALCIUM-BINDING DOMAIN; CARDIAC ARRHYTHMIA; CARDIAC TISSUES; CHANNEL FUNCTIONS; EF-HAND; HELIX BUNDLE; HETERONUCLEAR; HIGH AFFINITY BINDING; INACTIVATION GATING; INTRACELLULAR CALCIUM; ISOTHERMAL TITRATION CALORIMETRY; MOLECULAR BASIS; SODIUM CHANNEL; SOLUTION NMR; SOLUTION STRUCTURES;

AMINES; CALCIUM; CALCIUM ALLOYS; LAWS AND LEGISLATION; NUCLEAR MAGNETIC RESONANCE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PLANTS (BOTANY); PROTEINS; SODIUM;

MAGNETIC DOMAINS;

CALCIUM; CALCIUM SENSING RECEPTOR; CALMODULIN; VOLTAGE GATED SODIUM CHANNEL; CALCIUM BINDING PROTEIN; MUSCLE PROTEIN; PEPTIDE; SCN5A PROTEIN, HUMAN; SODIUM CHANNEL;

ACTION POTENTIAL; AMINO ACID SEQUENCE; ARTICLE; BINDING AFFINITY; CALCIUM BINDING; CALCIUM CELL LEVEL; CALCIUM SIGNALING; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; HEART; HEART ARRHYTHMIA; HUMAN; HUMAN TISSUE; ISOTHERMAL TITRATION CALORIMETRY; MUTATION; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN ISOLATION; PROTEIN LOCALIZATION; PROTEIN MOTIF; PROTEIN STRUCTURE; REGULATORY MECHANISM; CHEMISTRY; GENETICS; HEART MUSCLE; METABOLISM; NUCLEAR MAGNETIC RESONANCE; PHYSIOLOGY; PROTEIN BINDING; PROTEIN TERTIARY STRUCTURE; SYNDROME;

AMINO ACID MOTIFS; ARRHYTHMIAS, CARDIAC; CALCIUM; CALCIUM-BINDING PROTEINS; CALMODULIN; HUMANS; MUSCLE PROTEINS; MYOCARDIUM; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDES; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; SODIUM CHANNELS; SYNDROME;

EID: 65249136569     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M807747200     Document Type: Article

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