Charged residues in transmembrane domains II and XI of a vesicular monoamine transporter form a charge pair that promotes high affinity substrate recognition

Journal of Biological Chemistry

Volumn 272, Issue 9, 1997, Pages 5403-5408

  Merickel, Andrew ^a   Kaback, H Ronald ^b   Edwards, Robert H ^c  

^a Interdepartmental PhD Program for Neuroscience   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

MONOAMINE; RESERPINE; SEROTONIN;

AMINO ACID SUBSTITUTION; ARTICLE; BINDING AFFINITY; BINDING SITE; CELL MEMBRANE TRANSPORT; ESCHERICHIA COLI; MEMBRANE VESICLE; NEUROTRANSMITTER RELEASE; NONHUMAN; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS;

ANIMALS; ASPARAGINE; ASPARTIC ACID; BIOLOGICAL TRANSPORT; CARBONYL CYANIDE M-CHLOROPHENYL HYDRAZONE; HUMANS; KINETICS; LYSINE; MEMBRANE GLYCOPROTEINS; MEMBRANE TRANSPORT PROTEINS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; NEUROPEPTIDES; NEUROTRANSMITTER AGENTS; RATS; RESERPINE; SEROTONIN; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY; VESICULAR BIOGENIC AMINE TRANSPORT PROTEINS; VESICULAR MONOAMINE TRANSPORT PROTEINS;

ESCHERICHIA COLI;

EID: 0031054527     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.272.9.5403     Document Type: Article

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