Calmodulin's flexibility allows for promiscuity in its interactions with target proteins and peptides

Applied Biochemistry and Biotechnology - Part B Molecular Biotechnology

Volumn 27, Issue 1, 2004, Pages 33-57

  Yamniuk, Aaron P ^b   Vogel, Hans J ^a  

^a UNIVERSITY OF CALGARY   (Canada)

^b NONE

Author keywords

Calcium; Calmodulin; Calmodulin binding peptide; Protein structure; Target protein

Indexed keywords

BIODIVERSITY; CALCIUM; CONFORMATIONS; HYDROPHOBICITY; IONS; PLANTS (BOTANY);

CADMODULIN-BINDING PEPTIDE; CALMODULIN; PROTEIN STRUCTURE; TARGET PROTEIN;

ENZYMES;

CALCIUM; CALMODULIN; HELIX LOOP HELIX PROTEIN; METHIONINE; PEPTIDASE; PROTEIN; FUNGAL PROTEIN; ISOPROTEIN; VEGETABLE PROTEIN;

AMINO ACID SEQUENCE; CALCIUM BINDING; CALCIUM CELL LEVEL; CRYSTAL STRUCTURE; ENZYME ACTIVATION; ENZYME REGULATION; HYDROPHOBICITY; MOLECULAR RECOGNITION; NONHUMAN; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; PROTEIN TARGETING; REVIEW; ANIMAL; BINDING SITE; CHEMISTRY; GENETICS; HUMAN; METABOLISM; MOLECULAR GENETICS; PROTEIN MOTIF;

MAMMALIA;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CALCIUM; CALMODULIN; FUNGAL PROTEINS; HUMANS; MOLECULAR SEQUENCE DATA; PLANT PROTEINS; PROTEIN ISOFORMS; PROTEINS;

EID: 1942496481     PISSN: 10736085     EISSN: None     Source Type: Journal    
DOI: 10.1385/mb:27:1:33     Document Type: Review

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