Structural basis of the significant calmodulin-induced increase in the enzymatic activity of secreted phospholipases A2

Protein Engineering, Design and Selection

Volumn 23, Issue 6, 2010, Pages 479-487

  Kovačič, Lidija ^a   Novinec, Marko ^a   Petan, Toni ^a   Križaj, Igor ^a  

^a JO EF STEFAN INSTITUTE   (Slovenia)

Author keywords

ammodytoxin; CaM; complex; protein docking; sPLA2

Indexed keywords

ACTIVITY ENHANCEMENT; DOCKING ALGORITHMS; ENZYMATIC ACTIVITIES; INTERACTION SITE; ISOFORMS; PATHOPHYSIOLOGY; PHOSPHOLIPASE A2; PHOSPHOLIPASES; PROTEIN DOCKING; REDUCING CONDITIONS; SNAKE VENOMS; STABLE COMPLEXES; STRUCTURAL BASIS;

CALMODULIN; COMPLEXATION; DOCKING; ENZYMES; MAMMALS; PLANTS (BOTANY); STABILIZATION;

CAMS;

AMMODYTOXIN A; CALMODULIN; PHOSPHOLIPASE A2;

ALGORITHM; ARTICLE; BINDING SITE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME STRUCTURE; MAMMAL; MUTAGENESIS; NONHUMAN; PATHOPHYSIOLOGY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FUNCTION; STRUCTURE ANALYSIS; VALIDATION STUDY;

ALGORITHMS; AMINO ACID SEQUENCE; ANIMALS; CALMODULIN; GROUP II PHOSPHOLIPASES A2; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; VIPER VENOMS; VIPERIDAE;

MAMMALIA;

EID: 77955178920     PISSN: 17410126     EISSN: 17410134     Source Type: Journal    
DOI: 10.1093/protein/gzq019     Document Type: Article

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