A high-affinity calmodulin-binding site in a tobacco plasma-membrane channel protein coincides with a characteristic element of cyclic nucleotide-binding domains

Plant Molecular Biology

Volumn 42, Issue 4, 2000, Pages 591-601

  Arazi, Tzahi ^a   Kaplan, Boaz ^a   Fromm, Hillel ^a,b  

^a WEIZMANN INSTITUTE OF SCIENCE   (Israel)

^b UNIVERSITY OF LEEDS   (United Kingdom)

Author keywords

CaM binding channel; cAMP dependent kinase; Dansyl CaM; Olfactory channel; Two hybrid system

Indexed keywords

AMINO ACID SEQUENCE; ANTIBODY SPECIFICITY; BINDING SITE; CALMODULIN BINDING CHANNEL PROTEIN; CALMODULIN; COMPLEMENTARY DNA; COMPLEX FORMATION; DISSOCIATION CONSTANT; FLUORESCENCE; PROTEIN DETECTION; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN PROTEIN INTERACTION; RECOMBINANT PROTEIN; SIGNAL TRANSDUCTION; SOLUBILIZATION; TOBACCO;

AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; BINDING, COMPETITIVE; CALCIUM; CALMODULIN; CALMODULIN-BINDING PROTEINS; CATTLE; CELL LINE; CYCLIC AMP; CYCLIC AMP-DEPENDENT PROTEIN KINASES; GLUTATHIONE TRANSFERASE; MEMBRANE PROTEINS; MOLECULAR SEQUENCE DATA; NUCLEOTIDES, CYCLIC; PLANT PROTEINS; PLANTS, TOXIC; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; RATS; RECOMBINANT FUSION PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; TOBACCO;

ANIMALIA; INSECTA; MAMMALIA; NICOTIANA TABACUM;

EID: 0034012321     PISSN: 01674412     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1006345302589     Document Type: Article

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