Plasticity in protein-DNA recognition: lac repressor interacts with its natural operator O1 through alternative conformations of its DNA-binding domain

EMBO Journal

Volumn 21, Issue 12, 2002, Pages 2866-2876

  Kalodimos, Charalampos G ^a   Bonvin, Alexandre M J J ^a   Salinas, Roberto K ^a   Wechselberger, Rainer ^a   Boelens, Rolf ^a   Kaptein, Robert ^a  

^a UTRECHT UNIVERSITY   (Netherlands)

Author keywords

Asymmetric DNA binding; DNA deformation; Lac repressor; Natural lac operator; NMR structure

Indexed keywords

DNA; REPRESSOR PROTEIN;

ALLOSTERISM; ARTICLE; DNA CONFORMATION; DNA PROTEIN COMPLEX; DNA SEQUENCE; GENE REARRANGEMENT; LACTOSE OPERON; MOLECULAR RECOGNITION; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN DNA BINDING; PROTEIN DNA INTERACTION; PROTEIN STRUCTURE; REPRESSOR GENE;

BACTERIAL PROTEINS; BINDING SITES; DIMERIZATION; DNA; ESCHERICHIA COLI PROTEINS; LAC OPERON; MODELS, MOLECULAR; NUCLEIC ACID CONFORMATION; OPERATOR REGIONS (GENETICS); PROTEIN BINDING; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; REPRESSOR PROTEINS;

EID: 0037124326     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/cdf318     Document Type: Article

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