The induction of folding cooperativity by ligand binding drives the allosteric response of tetracycline repressor

Proceedings of the National Academy of Sciences of the United States of America

Volumn 106, Issue 52, 2009, Pages 22263-22268

  Reichheld, Sean E ^a   Yu, Zhou ^a   Davidson, Alan R ^a  

^a UNIVERSITY OF TORONTO   (Canada)

Author keywords

Allostery; DNA binding; Drug binding

Indexed keywords

HOMODIMER; REPRESSOR PROTEIN; TETRACYCLINE; TETRACYCLINE REPRESSOR PROTEIN; UNCLASSIFIED DRUG;

ALLOSTERISM; ARTICLE; CONFORMATION; DIMERIZATION; DNA BINDING; LIGAND BINDING; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FOLDING; THERMODYNAMICS; WILD TYPE;

ALLOSTERIC REGULATION; BASE SEQUENCE; BINDING SITES; BIOPHYSICAL PHENOMENA; DNA, BACTERIAL; ESCHERICHIA COLI PROTEINS; KINETICS; LIGANDS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE, TERTIARY; REPRESSOR PROTEINS; TETRACYCLINE; THERMODYNAMICS;

EID: 76049113822     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0911566106     Document Type: Article

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