Structural elements within the methylation loop (residues 112-117) and EF hands III and IV of calmodulin are required for Lys115 trimethylation

Biochemical Journal

Volumn 340, Issue 2, 1999, Pages 417-424

  Cobb, Jennifer A ^a   Han, Chang Hoon ^a   Wills, David M ^a   Roberts, Daniel M ^a  

^a UNIVERSITY OF TENNESSEE   (United States)

Author keywords

Calcium; Methyltransferase; NAD+ kinase

Indexed keywords

ALANINE; CALMODULIN; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; GLUTAMINE; HELIX LOOP HELIX PROTEIN; LEUCINE; LYSINE; METHYLTRANSFERASE; MUTANT PROTEIN; NICOTINAMIDE ADENINE DINUCLEOTIDE KINASE; THREONINE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME INHIBITION; POINT MUTATION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN METHYLATION; PROTEIN STRUCTURE; SITE DIRECTED MUTAGENESIS;

BASE SEQUENCE; CALMODULIN; CLONING, MOLECULAR; DNA PRIMERS; ENZYME ACTIVATION; METHYLATION; MUTAGENESIS, SITE-DIRECTED; POINT MUTATION;

EID: 0033153492     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/0264-6021:3400417     Document Type: Article

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