The gate of the influenza virus M2 proton channel is formed by a single tryptophan residue

Journal of Biological Chemistry

Volumn 277, Issue 42, 2002, Pages 39880-39886

  Tang, Yajun ^a   Zaitseva, Florina ^a   Lamb, Robert A ^a   Pinto, Lawrence H ^a  

^a NORTHWESTERN UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MEMBRANES; PH EFFECTS; PROTEINS; PROTONS;

PROTON CHANNELS;

VIRUSES;

CELL PROTEIN; COPPER ION; ION CHANNEL; ION CHANNEL PROTEIN M2; TRYPTOPHAN; UNCLASSIFIED DRUG;

ACIDIFICATION; ANIMAL CELL; ARTICLE; CELL MEMBRANE; CELL PH; CHANNEL GATING; CONTROLLED STUDY; ENDOSOME; FEMALE; INFLUENZA VIRUS; MEMBRANE CURRENT; NONHUMAN; OOCYTE; POROSITY; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN STRUCTURE; VIRION;

ANIMALS; CELL MEMBRANE; CYSTEINE; DNA, COMPLEMENTARY; HISTIDINE; HYDROGEN-ION CONCENTRATION; IONS; KINETICS; MEMBRANE POTENTIALS; MESYLATES; MUTATION; OOCYTES; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; TIME FACTORS; TRYPTOPHAN; VIRAL MATRIX PROTEINS; XENOPUS LAEVIS;

ANIMALIA; INFLUENZA VIRUS; RNA VIRUSES;

EID: 0037131381     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M206582200     Document Type: Article

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