Methionine to glutamine substitutions in the C-terminal domain of calmodulin impair the activation of three protein kinases

Journal of Biological Chemistry

Volumn 271, Issue 48, 1996, Pages 30465-30471

  Chin, David ^a   Means, Anthony R ^a  

^a DUKE UNIVERSITY MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CALMODULIN; GLUTAMINE; METHIONINE; MUTANT PROTEIN; MYOSIN LIGHT CHAIN KINASE; PROTEIN KINASE; PROTEIN KINASE (CALCIUM,CALMODULIN); PROTEIN KINASE (CALCIUM,CALMODULIN) II;

AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; BINDING AFFINITY; CARBOXY TERMINAL SEQUENCE; CIRCULAR DICHROISM; CONTROLLED STUDY; DNA SEQUENCE; ENZYME ACTIVATION; ENZYME ASSAY; ENZYME BINDING; ENZYME PHOSPHORYLATION; FLUORESCENCE SPECTROSCOPY; HYDROPHOBICITY; NONHUMAN; POINT MUTATION; PRIORITY JOURNAL;

AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CA(2+)-CALMODULIN DEPENDENT PROTEIN KINASE; CALCIUM; CALMODULIN; ENZYME ACTIVATION; GLUTAMINE; KINETICS; METHIONINE; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; MYOSIN-LIGHT-CHAIN KINASE; PEPTIDES; PHOSPHORYLATION; PROTEIN BINDING; STRUCTURE-ACTIVITY RELATIONSHIP;

ANIMALIA; VERTEBRATA;

EID: 0029803672     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.271.48.30465     Document Type: Article

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