The N terminus of connexin37 contains an α-helix that is required for channel function

Journal of Biological Chemistry

Volumn 284, Issue 30, 2009, Pages 20418-20427

  Kyle, John W ^a   Berthoud, Viviana M ^a   Kurutz, Josh ^a   Minogue, Peter J ^a   Greenspan, Michael ^a   Hanck, Dorothy A ^a   Beyer, Eric C ^a  

^a UNIVERSITY OF CHICAGO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CHANNEL FUNCTIONS; CHANNEL GATING; CIRCULAR DICHROISM; DOUBLE SUBSTITUTION; GAP JUNCTIONS; HELA CELL; HELICAL STRUCTURES; N-TERMINAL; N-TERMINAL DOMAINS; NUCLEAR MAGNETIC RESONANCE STUDIES; PROTEIN LOCALIZATION; SYNTHETIC PEPTIDE; WILD TYPES; XENOPUS OOCYTE;

AMINATION; AMINES; DICHROISM; NUCLEAR MAGNETIC RESONANCE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; ORGANIC ACIDS;

AMINO ACIDS;

ALANINE; AMINO ACID DERIVATIVE; CONNEXIN 37; GLUTAMIC ACID; GLUTAMINE; GLYCINE; LEUCINE; MUTANT PROTEIN; PROLINE;

ALPHA HELIX; AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; CONTROLLED STUDY; FEMALE; GENETIC TRANSFECTION; HUMAN; HUMAN CELL; NONHUMAN; OOCYTE; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN LOCALIZATION; SITE DIRECTED MUTAGENESIS;

AMINO ACID SEQUENCE; ANIMALS; BIOTIN; CIRCULAR DICHROISM; CONNEXINS; GAP JUNCTIONS; HELA CELLS; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; OOCYTES; PEPTIDES; PROTEIN STRUCTURE, SECONDARY; XENOPUS;

EID: 67749086698     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.016907     Document Type: Article

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