A basic cluster determines topology of the cytoplasmic M3-M4 loop of the glycine receptor α1 subunit

Journal of Biological Chemistry

Volumn 278, Issue 19, 2003, Pages 16782-16790

  Sadtler, Sven ^a   Laube, Bodo ^b   Lashub, Alhassan ^b   Nicke, Annette ^a   Betz, Heinrich ^b   Schmalzing, Günther ^a,c  

^a RWTH AACHEN UNIVERSITY   (Germany)

^b MAX PLANCK INSTITUTE FOR BRAIN RESEARCH   (Germany)

^c Dept of Molecular Pharmacology ^*  (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ANIMAL CELL CULTURE; CELL MEMBRANES; MOLECULAR STRUCTURE; NEUROLOGY; TOPOLOGY;

NEUROTRANSMITTERS;

BIOCHEMICAL ENGINEERING;

COMPLEMENTARY DNA; GLYCINE RECEPTOR; ION CHANNEL; RECEPTOR SUBUNIT; GLYCINE RECEPTOR ALPHA1;

AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; CYTOPLASM; ENDOPLASMIC RETICULUM; GENE EXPRESSION; NEUROTRANSMISSION; NONHUMAN; OOCYTE; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN PURIFICATION; XENOPUS; AMINO ACID SEQUENCE; ANIMAL; CELL MEMBRANE; CHEMISTRY; GENETICS; HUMAN; MOLECULAR GENETICS; MUTATION; PROTEIN CONFORMATION; STRUCTURE ACTIVITY RELATION;

ANIMALIA;

AMINO ACID SEQUENCE; ANIMALS; CELL MEMBRANE; HUMANS; MOLECULAR SEQUENCE DATA; MUTATION; PROTEIN CONFORMATION; RECEPTORS, GLYCINE; STRUCTURE-ACTIVITY RELATIONSHIP; XENOPUS;

EID: 0037931744     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M213077200     Document Type: Article

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