Structural, biochemical, and functional characterization of the cyclic nucleotide binding homology domain from the mouse EAG1 potassium channel

Journal of Molecular Biology

Volumn 423, Issue 1, 2012, Pages 34-46

  Marques Carvalho, Maria J ^a,b   Sahoo, Nirakar ^c   Muskett, Frederick W ^d   Vieira Pires, Ricardo S ^a   Gabant, Guillaume ^e   Cadene, Martine ^e   Schönherr, Roland ^c   Morais Cabral, João H ^a  

^a UNIVERSITY OF PORTO   (Portugal)

^b UNIVERSITY OF PORTO   (Portugal)

^c JENA UNIVERSITY HOSPITAL   (Germany)

^d UNIVERSITY OF LEICESTER   (United Kingdom)

^e CENTRE DE BIOPHYSIQUE MOLÉCULAIRE   (France)

Author keywords

calmodulin; CNB domain; CNB homology domain; crystal structure

Indexed keywords

ARGININE; CALMODULIN; CYCLIC NUCLEOTIDE; CYSTEINE; POTASSIUM CHANNEL HERG; TYROSINE; VOLTAGE GATED POTASSIUM CHANNEL;

ALPHA HELIX; ANIMAL CELL; ARTICLE; BINDING AFFINITY; BINDING SITE; CARBOXY TERMINAL SEQUENCE; CHANNEL GATING; CONTROLLED STUDY; CYCLIC NUCLEOTIDE BINDING HOMOLOGY DOMAIN; ELECTROPHYSIOLOGY; HYPERPOLARIZATION; IN VITRO STUDY; LIGAND BINDING; MUTAGENESIS; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN PHOSPHORYLATION; PROTEIN STRUCTURE;

DANIO RERIO;

EID: 84866343022     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2012.06.025     Document Type: Article

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