The solution structures of two soybean calmodulin isoforms provide a structural basis for their selective target activation properties

Journal of Biological Chemistry

Volumn 283, Issue 21, 2008, Pages 14619-14628

  Ishida, Hiroaki ^a   Huang, Hao ^a   Yamniuk, Aaron P ^a   Takaya, Yoshiaki ^a,b   Vogel, Hans J ^a  

^a UNIVERSITY OF CALGARY   (Canada)

^b MEIJO UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

AMINES; AMINO ACIDS; ANIMALS; BIOCHEMISTRY; CALCIUM ALLOYS; CAMS; CHEMICAL ACTIVATION; ENZYMES; NUCLEAR MAGNETIC RESONANCE; ORGANIC ACIDS; PHYSIOLOGICAL MODELS; TARGETS;

AMINO ACID SEQUENCES; BINDING PROTEINS; BIOPHYSICAL MEASUREMENTS; ENZYME ACTIVATIONS; EUKARYOTIC CELLS; HIGH RESOLUTIONS; IN PLANTS; INTRACELLULAR CALCIUMS; ISOFORM; ISOFORMS; OPEN CONFORMATIONS; PHYSIOLOGICAL FUNCTIONS; PHYSIOLOGICAL RESPONSES; PROTEIN BINDINGS; SEQUENCE IDENTITIES; SOLUTION STRUCTURES; STRUCTURAL BASES; STRUCTURAL DIFFERENCES; SYNTHASE; TARGET ACTIVATIONS;

CALCIUM;

CALMODULIN; NITRIC OXIDE SYNTHASE; PROTEIN SCAM1; PROTEIN SCAM4; UNCLASSIFIED DRUG; ISOPROTEIN;

AMINO ACID SEQUENCE; ARTICLE; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN EXPRESSION; PROTEIN STRUCTURE; SOYBEAN; CALORIMETRY; CHEMICAL STRUCTURE; CHEMISTRY; GENETICS; HYDROPHOBICITY; METABOLISM; MOLECULAR GENETICS; PROTEIN TERTIARY STRUCTURE; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY; SURFACE PROPERTY;

ANIMALIA; EUKARYOTA; GLYCINE MAX;

AMINO ACID SEQUENCE; CALMODULIN; CALORIMETRY; HYDROPHOBICITY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN ISOFORMS; PROTEIN STRUCTURE, TERTIARY; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; SOYBEANS; SURFACE PROPERTIES;

EID: 47249088656     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M801398200     Document Type: Article

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