Recognition of β-calcineurin by the domains of calmodulin: Thermodynamic and structural evidence for distinct roles

Proteins: Structure, Function and Bioinformatics

Volumn 79, Issue 3, 2011, Pages 765-786

  O'Donnell, Susan E ^a   Yu, Liping ^a   Fowler, C Andrew ^a   Shea, Madeline A ^a  

^a UNIVERSITY OF IOWA   (United States)

Author keywords

Allostery; Binding; Calcium; Energetics; Fluorescence; NMR; Stoichiometry

Indexed keywords

BETA CALCINEURIN; CALCINEURIN; CALMODULIN; MELITTIN; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; CALCIUM BINDING; CONFORMATIONAL TRANSITION; DISSOCIATION CONSTANT; HYDRODYNAMICS; LINKAGE ANALYSIS; NUCLEAR OVERHAUSER EFFECT; PRIORITY JOURNAL; PROTEIN BINDING; STOICHIOMETRY; THERMODYNAMICS;

AMINO ACID SEQUENCE; CALCINEURIN; CALMODULIN; LIGANDS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN CONFORMATION; SEQUENCE HOMOLOGY, AMINO ACID; THERMODYNAMICS;

CANA;

EID: 79551474570     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22917     Document Type: Article

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