The conformational plasticity of calmodulin upon calcium complexation gives a model of its interaction with the oedema factor of Bacillus anthracis

Proteins: Structure, Function and Genetics

Volumn 71, Issue 4, 2008, Pages 1813-1829

  Laine, Elodie ^a   Yoneda, Julliane D ^b   Blondel, Arnaud ^a   Malliavin, Thérèse E ^a  

^a INSTITUT PASTEUR   (France)

^b FLUMINENSE FEDERAL UNIVERSITY   (Brazil)

Author keywords

Bacillus anthracis; Calcium; Calmodulin; Essential dynamics; Molecular dynamics; NMR; Oedema factor; Solvent accessible surface

Indexed keywords

BACTERIAL PROTEIN; CALCIUM ION; CALMODULIN; EDEMA FACTOR;

AMINO TERMINAL SEQUENCE; ARTICLE; BACILLUS ANTHRACIS; CALCIUM BINDING; CARBOXY TERMINAL SEQUENCE; COMPLEX FORMATION; CONFORMATIONAL TRANSITION; MATHEMATICAL COMPUTING; MOLECULAR DYNAMICS; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN INTERACTION; PROTEIN STRUCTURE; SIMULATION;

AMINO ACID SEQUENCE; ANTIGENS, BACTERIAL; BACILLUS ANTHRACIS; BACTERIAL TOXINS; CALCIUM; CALMODULIN; COMPUTER SIMULATION; ELECTROSTATICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PRESSURE; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; TEMPERATURE; TIME FACTORS; WATER;

BACILLUS ANTHRACIS;

EID: 44349088854     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21862     Document Type: Article

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