Conformational differences between the wild type and V30M mutant transthyretin modulate its binding to genistein: Implications to tetramer stability and ligand-binding

Journal of Structural Biology

Volumn 170, Issue 3, 2010, Pages 522-531

  Trivella, Daniela B B ^a   Bleicher, Lucas ^a   Palmieri, Leonardo de Castro ^b   Wiggers, Helton José ^a   Montanari, Carlos Alberto ^a   Kelly, Jeffery W ^c   Lima, Luís Maurício T R ^b   Foguel, Débora ^b   Polikarpov, Igor ^a  

^a UNIVERSITY OF SÃO PAULO   (Brazil)

^b FEDERAL UNIVERSITY OF RIO DE JANEIRO   (Brazil)

^c SCRIPPS RESEARCH INSTITUTE   (United States)

Author keywords

Crystal structure; Genistein; Isothermal titration calorimetry; Pressure stability; V30M mutant TTR; Wild type TTR

Indexed keywords

GENISTEIN; MUTANT PROTEIN; PREALBUMIN;

ARTICLE; BINDING SITE; CONCENTRATION RESPONSE; CONTROLLED STUDY; CRYSTAL STRUCTURE; CRYSTALLIZATION; DRUG PROTEIN BINDING; HYDROSTATIC PRESSURE; ISOTHERMAL TITRATION CALORIMETRY; LIGAND BINDING; MOLECULAR RECOGNITION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN STABILITY; WILD TYPE;

ALLOSTERIC SITE; AMINO ACID SUBSTITUTION; AMYLOID; AMYLOIDOSIS; CRYSTALLOGRAPHY, X-RAY; GENISTEIN; HUMANS; HYDROGEN-ION CONCENTRATION; HYDROSTATIC PRESSURE; LIGANDS; MODELS, MOLECULAR; MUTANT PROTEINS; PREALBUMIN; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STABILITY; PROTEIN STRUCTURE, QUATERNARY; RECOMBINANT PROTEINS; THERMODYNAMICS;

EID: 77952671938     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2010.03.002     Document Type: Article

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